The Asymmetric Binding of PGC-1α to the ERRα and ERRγ Nuclear Receptor Homodimers Involves a Similar Recognition Mechanism
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{"title"=>"The Asymmetric Binding of PGC-1α to the ERRα and ERRγ Nuclear Receptor Homodimers Involves a Similar Recognition Mechanism", "type"=>"journal", "authors"=>[{"first_name"=>"Maria", "last_name"=>"Takacs", "scopus_author_id"=>"55787793200"}, {"first_name"=>"Maxim V.", "last_name"=>"Petoukhov", "scopus_author_id"=>"6603062919"}, {"first_name"=>"R. Andrew", "last_name"=>"Atkinson", "scopus_author_id"=>"7402373186"}, {"first_name"=>"Pierre", "last_name"=>"Roblin", "scopus_author_id"=>"7006807459"}, {"first_name"=>"François Xavier", "last_name"=>"Ogi", "scopus_author_id"=>"6507634747"}, {"first_name"=>"Borries", "last_name"=>"Demeler", "scopus_author_id"=>"7004087211"}, {"first_name"=>"Noelle", "last_name"=>"Potier", "scopus_author_id"=>"6603833645"}, {"first_name"=>"Yassmine", "last_name"=>"Chebaro", "scopus_author_id"=>"26321045700"}, {"first_name"=>"Annick", "last_name"=>"Dejaegere", "scopus_author_id"=>"56144660300"}, {"first_name"=>"Dmitri I.", "last_name"=>"Svergun", "scopus_author_id"=>"18134896800"}, {"first_name"=>"Dino", "last_name"=>"Moras", "scopus_author_id"=>"7102899054"}, {"first_name"=>"Isabelle M.L.", "last_name"=>"Billas", "scopus_author_id"=>"57197848682"}], "year"=>2013, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-84879992086", "doi"=>"10.1371/journal.pone.0067810", "sgr"=>"84879992086", "isbn"=>"1932-6203 (Electronic)\r1932-6203 (Linking)", "pmid"=>"23874451", "issn"=>"19326203", "pui"=>"369287131"}, "id"=>"7789b5ed-2a3b-327a-9594-e4381805f2f1", "abstract"=>"BACKGROUND: PGC-1α is a crucial regulator of cellular metabolism and energy homeostasis that functionally acts together with the estrogen-related receptors (ERRα and ERRγ) in the regulation of mitochondrial and metabolic gene networks. Dimerization of the ERRs is a pre-requisite for interactions with PGC-1α and other coactivators, eventually leading to transactivation. It was suggested recently (Devarakonda et al) that PGC-1α binds in a strikingly different manner to ERRγ ligand-binding domains (LBDs) compared to its mode of binding to ERRα and other nuclear receptors (NRs), where it interacts directly with the two ERRγ homodimer subunits.\\n\\nMETHODS/PRINCIPAL FINDINGS: Here, we show that PGC-1α receptor interacting domain (RID) binds in an almost identical manner to ERRα and ERRγ homodimers. Microscale thermophoresis demonstrated that the interactions between PGC-1α RID and ERR LBDs involve a single receptor subunit through high-affinity, ERR-specific L3 and low-affinity L2 interactions. NMR studies further defined the limits of PGC-1α RID that interacts with ERRs. Consistent with these findings, the solution structures of PGC-1α/ERRα LBDs and PGC-1α/ERRγ LBDs complexes share an identical architecture with an asymmetric binding of PGC-1α to homodimeric ERR.\\n\\nCONCLUSIONS/SIGNIFICANCE: These studies provide the molecular determinants for the specificity of interactions between PGC-1α and the ERRs, whereby negative cooperativity prevails in the binding of the coactivators to these receptors. Our work indicates that allosteric regulation may be a general mechanism controlling the binding of the coactivators to homodimers.", "link"=>"http://www.mendeley.com/research/asymmetric-binding-pgc1%CE%B1-err%CE%B1-err%CE%B3-nuclear-receptor-homodimers-involves-similar-recognition-mechanis", "reader_count"=>33, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Student > Doctoral Student"=>2, "Researcher"=>10, "Student > Ph. D. Student"=>8, "Student > Postgraduate"=>1, "Other"=>4, "Student > Master"=>2, "Student > Bachelor"=>3, "Professor"=>2}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Student > Doctoral Student"=>2, "Researcher"=>10, "Student > Ph. D. Student"=>8, "Student > Postgraduate"=>1, "Other"=>4, "Student > Master"=>2, "Student > Bachelor"=>3, "Professor"=>2}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Biochemistry, Genetics and Molecular Biology"=>6, "Agricultural and Biological Sciences"=>15, "Medicine and Dentistry"=>4, "Chemistry"=>5, "Computer Science"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>4}, "Chemistry"=>{"Chemistry"=>5}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>15}, "Computer Science"=>{"Computer Science"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>6}, "Unspecified"=>{"Unspecified"=>2}}, "reader_count_by_country"=>{"Japan"=>1, "Italy"=>1}, "group_count"=>3}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1114722"], "description"=>"<p>PGC-1α contains three LxxLL motifs, two of which (L2 and L3) are responsible for specific interaction with NRs. The protein constructs used here are PGC-1α RID1 (122–235), PGC-1α RID2 (122–285) and PGC-1α NTD (1–285) that contain motifs L2 and L3. On the right, the sequence of the His<sub>6</sub>-tagged PGC-1α RID2 is given showing residues of the L2 and L3 motifs (bold, blue). Residues identified by NMR as being outside the interacting region are shown in green; residues unambiguously identified as being in the interacting region are shown in red; additional candidate Ser/Thr residues, affected by binding are underlined.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "cofactors", "hormones", "biophysics", "Macromolecular assemblies", "Computational biology", "Macromolecular structure analysis", "protein structure", "Molecular cell biology", "Signal transduction", "Nuclear receptor signaling", "Endocrinology", "oncology", "Basic cancer research", "constructs"], "article_id"=>742209, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Mária Takács", "Maxim V. Petoukhov", "R. Andrew Atkinson", "Pierre Roblin", "François-Xavier Ogi", "Borries Demeler", "Noelle Potier", "Yassmine Chebaro", "Annick Dejaegere", "Dmitri I. Svergun", "Dino Moras", "Isabelle M. L. Billas"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0067810.g001", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Architecture_of_human_PGC_1_945_and_constructs_used_in_this_study_/742209", "title"=>"Architecture of human PGC-1α and constructs used in this study.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-09 02:27:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/1114723"], "description"=>"<p>NMR spectra of PGC-1α RID fragments in interaction with (<b>A–B</b>) ERRα LBD and (<b>C</b>) ERRγ LBD. <sup>1</sup>H-<sup>15</sup>N HSQC spectra of PGC-1α RID1 (<b>A and C</b>) and RID2 (<b>B</b>) alone (black) and following addition of unlabeled ERR LBD (red). The sets of attenuated cross-peaks are broadly similar. The additional peaks in RID2 are not affected by binding to either ERR LBD. Cross-peaks in regions expected for Gly and Ser/Thr residues are boxed and the cross-peak that probably arises from the C-ter residue is indicated (CT). The cross-peak corresponding to W189 is boxed, showing the broadening or shift upon complex formation.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "cofactors", "hormones", "biophysics", "Macromolecular assemblies", "Computational biology", "Macromolecular structure analysis", "protein structure", "Molecular cell biology", "Signal transduction", "Nuclear receptor signaling", "Endocrinology", "oncology", "Basic cancer research", "interacts"], "article_id"=>742210, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Mária Takács", "Maxim V. Petoukhov", "R. Andrew Atkinson", "Pierre Roblin", "François-Xavier Ogi", "Borries Demeler", "Noelle Potier", "Yassmine Chebaro", "Annick Dejaegere", "Dmitri I. Svergun", "Dino Moras", "Isabelle M. L. Billas"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0067810.g002", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PGC_1_945_RID_interacts_through_an_identical_region_with_ERR_945_and_ERR_947_LBD_/742210", "title"=>"PGC-1α RID interacts through an identical region with ERRα and ERRγ LBD.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-09 02:27:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/1114724"], "description"=>"<p><b>A</b> and <b>B</b>. SV-AUC experiments for a titration series of increasing molar ratio of PGC-1α RID2 with respect to (<b>A)</b> ERRα and (<b>B</b>) ERRγ LBD dimer. G(S<sub>20,w</sub>) distributions are shown over the entire boundary for free PGC-1α RID2 (green), free ERR LBD (red) and for the titration series with ERR LBD:PGC-1α RID2 ratios 1∶0.5 (blue), 1∶1.4 (black) and 1∶3 (magenta). The excess of PGC-1α RID2 in the 1∶3 data is seen as a shoulder extending to values close to that of free PGC-1α RID2. In the experiments with ERRγ LBD, the concentration of PGC-1α RID2 was overestimated, as can be seen by the faint shoulder of the 1∶3 titration data. Thus the 1∶1.4 molar ratio is overestimated and as a consequence the corresponding data approach a limiting value of saturation given by the 1∶3 titration data. <b>C</b> and <b>D</b>. ESI mass spectra recorded under non-denaturing conditions in 200 mM ammonium acetate at pH = 7.4 for (<b>C</b>) ERRα LBD (top) and PGC-1α RID2/ERRα (bottom) and for (<b>D</b>) ERRγ LBD (top) and PGC-1α RID2/ERRγ complex (bottom). The different charge states of the proteins are indicated above the peaks and depicted for ERRα and ERRγ with green and red dots, respectively and for PGC-1α RID2/ERRα and PGC-1α RID2/ERRγ with magenta and blue triangles, respectively. For the measurements of ERRα complexes, the His<sub>6</sub>-tag of ERRα LBD was not cleaved, resulting in an increase of 3766 Da with respect to the molecular weight shown in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0067810#pone.0067810.s007\" target=\"_blank\">Table S1</a>.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "cofactors", "hormones", "biophysics", "Macromolecular assemblies", "Computational biology", "Macromolecular structure analysis", "protein structure", "Molecular cell biology", "Signal transduction", "Nuclear receptor signaling", "Endocrinology", "oncology", "Basic cancer research", "characterization", "stoichiometry"], "article_id"=>742211, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Mária Takács", "Maxim V. Petoukhov", "R. Andrew Atkinson", "Pierre Roblin", "François-Xavier Ogi", "Borries Demeler", "Noelle Potier", "Yassmine Chebaro", "Annick Dejaegere", "Dmitri I. Svergun", "Dino Moras", "Isabelle M. L. Billas"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0067810.g003", "stats"=>{"downloads"=>5, "page_views"=>13, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Biophysical_characterization_of_the_stoichiometry_of_the_PGC_1_945_RID2_ERR_complexes_/742211", "title"=>"Biophysical characterization of the stoichiometry of the PGC-1α RID2/ERR complexes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-09 02:27:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/1114725"], "description"=>"<p>Unlabeled PGC-1α RID1 protein was titrated into a fixed concentration of (<b>A</b>) labeled ERRα LBD and (<b>B</b>) labeled ERRγ LBD. Top panels: raw thermophoresis data recorded at 20°C using the LED at 50% and IR-laser at 80%. Bottom panels: isotherms averaged over three consecutive measurements and fitted according to the law of mass action to yield the apparent K<sub>D,1</sub>. For the determination of K<sub>D,1</sub>, the concentration of unlabeled PGC-1α RID1 was varied between 30 µM and 3 nM, while the concentration of ERR LBD was kept fixed (50 nM). Insets: isotherms for titration series comprising higher unlabeled PGC-1α RID1 concentrations (300 µM to 10 nM) with a fixed ERR LBD concentration (20 nM), showing the two binding events of binding affinities K<sub>D,1</sub> and K<sub>D,2</sub>.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "cofactors", "hormones", "biophysics", "Macromolecular assemblies", "Computational biology", "Macromolecular structure analysis", "protein structure", "Molecular cell biology", "Signal transduction", "Nuclear receptor signaling", "Endocrinology", "oncology", "Basic cancer research", "rid1", "binding"], "article_id"=>742212, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Mária Takács", "Maxim V. Petoukhov", "R. Andrew Atkinson", "Pierre Roblin", "François-Xavier Ogi", "Borries Demeler", "Noelle Potier", "Yassmine Chebaro", "Annick Dejaegere", "Dmitri I. Svergun", "Dino Moras", "Isabelle M. L. Billas"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0067810.g004", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_PGC_1_945_RID1_binding_to_ERR_945_and_ERR_947_measured_by_MST_/742212", "title"=>"PGC-1α RID1 binding to ERRα and ERRγ measured by MST.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-09 02:27:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/1114726"], "description"=>"<p><b>A</b>. Scattering profiles of (from top to bottom) ERRγ LBD, PGC-1α RID1/ERRα, PGC-1α RID1/ERRγ, PGC-1α RID2/ERRγ and PGC-1α NTD/ERRγ. Experimental data are denoted by black dots, the corresponding fits are given as solid lines. Red fit is computed from the crystal structure of ERRγ LBD (PDB entry 1KV6). Blue fits are yielded by the best MD based model of PGC-1α RID1/ERRγ. Green lines represent the fits to the experimental data by the appropriate <i>ab initio</i> bead models. The profiles are arbitrary displaced in logarithmic scale for better visualization. <b>B</b>. Distance distribution functions of ERRγ LBD (red), PGC-1α RID1/ERRα (blue) PGC-1α RID1/ERRγ (green), PGC-1α RID2/ERRγ (magenta) and PGC-1α NTD/ERRγ (cyan) computed from the X-ray scattering patterns using the program GNOM. <b>C</b>. <i>Ab initio</i> molecular envelopes from SAXS measurements. The <i>ab initio</i> molecular envelope of ERRγ LBD alone is shown in semi-transparent red color together with the crystal structure of ERRγ LBD bound to short peptides derived from the coactivator SCR-1 (PDB code 1KV6). The <i>ab initio</i> molecular envelopes of the complexes between ERRγ LBD and PGC-1α RID1 (green), PGC-1α RID2 (magenta) and PGC-1α NTD (cyan) are depicted highlighting the location of the additional 50 amino acids at the C-terminal of the PGC-1α RID2 and of the N-terminal extension of PGC-1α NTD. The Cα-trace of ERRγ LBD homodimer and of the coactivator peptides are shown in grey and yellow ribbons, respectively.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "cofactors", "hormones", "biophysics", "Macromolecular assemblies", "Computational biology", "Macromolecular structure analysis", "protein structure", "Molecular cell biology", "Signal transduction", "Nuclear receptor signaling", "Endocrinology", "oncology", "Basic cancer research", "err"], "article_id"=>742213, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Mária Takács", "Maxim V. Petoukhov", "R. Andrew Atkinson", "Pierre Roblin", "François-Xavier Ogi", "Borries Demeler", "Noelle Potier", "Yassmine Chebaro", "Annick Dejaegere", "Dmitri I. Svergun", "Dino Moras", "Isabelle M. L. Billas"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0067810.g005", "stats"=>{"downloads"=>2, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_SAXS_of_ERR_and_ERR_in_complex_with_PGC_1_945_RID_/742213", "title"=>"SAXS of ERR and ERR in complex with PGC-1α RID.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-09 02:27:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/1114727"], "description"=>"<p><b>A</b>. and <b>B</b>. Schematic cartoon representations of the pseudo-atomic solution structures of the complex PGC-1α RID1/ERRγ. The Cα-trace of the PGC-1α RID1 molecule resulting from the rigid-body refinement is shown in light yellow. The N- and C-terminal ends and the positions of motifs L2 and L3, both of which corresponding to helices, are indicated. The Cα-trace of ERRγ LBD dimer is shown in dark grey (PDB entry 1KV6). <b>A</b>. One of the representative model obtained after relaxation using MD at moderate temperature is shown in blue. <b>B</b>. One of the representative model obtained along the trajectory of the higher temperature MD run is depicted in red. <b>C</b> and <b>D</b>. Molecular envelopes of the complexes PGC-1α RID1/ERRγ (green) and PGC-1α RID1/ERRα (blue) together with the pseudo-atomic solution structure of PGC-1α RID1/ERRγ shown in (A). The orientation of the models in C and D is identical to that in A and B.</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "cofactors", "hormones", "biophysics", "Macromolecular assemblies", "Computational biology", "Macromolecular structure analysis", "protein structure", "Molecular cell biology", "Signal transduction", "Nuclear receptor signaling", "Endocrinology", "oncology", "Basic cancer research"], "article_id"=>742214, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Mária Takács", "Maxim V. Petoukhov", "R. Andrew Atkinson", "Pierre Roblin", "François-Xavier Ogi", "Borries Demeler", "Noelle Potier", "Yassmine Chebaro", "Annick Dejaegere", "Dmitri I. Svergun", "Dino Moras", "Isabelle M. L. Billas"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0067810.g006", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Solution_structure_of_PGC_1_RID1_ERR_and_comparison_with_the_ab_initio_envelope_of_PGC_1_RID1_ERR_/742214", "title"=>"Solution structure of PGC-1α RID1/ERRγ and comparison with the <i>ab initio</i> envelope of PGC-1α RID1/ERRα.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-07-09 02:27:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/1114728"], "description"=>"<p>ITC data determined at 20°C and at pH = 7.5 as described in <i>SI.</i></p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "cofactors", "hormones", "biophysics", "Macromolecular assemblies", "Computational biology", "Macromolecular structure analysis", "protein structure", "Molecular cell biology", "Signal transduction", "Nuclear receptor signaling", "Endocrinology", "oncology", "Basic cancer research", "binding", "affinities", "lbd", "mst"], "article_id"=>742215, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Mária Takács", "Maxim V. Petoukhov", "R. Andrew Atkinson", "Pierre Roblin", "François-Xavier Ogi", "Borries Demeler", "Noelle Potier", "Yassmine Chebaro", "Annick Dejaegere", "Dmitri I. Svergun", "Dino Moras", "Isabelle M. L. Billas"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0067810.t001", "stats"=>{"downloads"=>2, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Apparent_binding_affinities_of_PGC_1_945_ERR_LBD_from_MST_and_ITC_/742215", "title"=>"Apparent binding affinities of PGC-1α/ERR LBD from MST and ITC.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-09 02:27:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/1114729"], "description"=>"*<p>From Guinier analysis.</p>#<p>From GNOM analysis.</p>&<p>n.d. non determined.</p>$<p>Size-exclusion chromatography(SEC) or Direct injection into SAXS cell (Direct).</p>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "cofactors", "hormones", "biophysics", "Macromolecular assemblies", "Computational biology", "Macromolecular structure analysis", "protein structure", "Molecular cell biology", "Signal transduction", "Nuclear receptor signaling", "Endocrinology", "oncology", "Basic cancer research", "complexes", "rids", "saxs"], "article_id"=>742216, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Mária Takács", "Maxim V. Petoukhov", "R. Andrew Atkinson", "Pierre Roblin", "François-Xavier Ogi", "Borries Demeler", "Noelle Potier", "Yassmine Chebaro", "Annick Dejaegere", "Dmitri I. Svergun", "Dino Moras", "Isabelle M. L. Billas"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0067810.t002", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structural_parameters_of_ERR_945_ERR_947_and_their_complexes_with_PGC_1_945_RIDs_from_SAXS_analysis_/742216", "title"=>"Structural parameters of ERRα, ERRγ and their complexes with PGC-1α RIDs from SAXS analysis.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-07-09 02:27:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/1114730", "https://ndownloader.figshare.com/files/1114731", "https://ndownloader.figshare.com/files/1114733", "https://ndownloader.figshare.com/files/1114738", "https://ndownloader.figshare.com/files/1114741", "https://ndownloader.figshare.com/files/1114742", "https://ndownloader.figshare.com/files/1114746", "https://ndownloader.figshare.com/files/1114750", "https://ndownloader.figshare.com/files/1114756", "https://ndownloader.figshare.com/files/1114759", "https://ndownloader.figshare.com/files/1114761"], "description"=>"<div><p>Background</p><p>PGC-1α is a crucial regulator of cellular metabolism and energy homeostasis that functionally acts together with the estrogen-related receptors (ERRα and ERRγ) in the regulation of mitochondrial and metabolic gene networks. Dimerization of the ERRs is a pre-requisite for interactions with PGC-1α and other coactivators, eventually leading to transactivation. It was suggested recently (Devarakonda <i>et al</i>) that PGC-1α binds in a strikingly different manner to ERRγ ligand-binding domains (LBDs) compared to its mode of binding to ERRα and other nuclear receptors (NRs), where it interacts directly with the two ERRγ homodimer subunits.</p><p>Methods/Principal Findings</p><p>Here, we show that PGC-1α receptor interacting domain (RID) binds in an almost identical manner to ERRα and ERRγ homodimers. Microscale thermophoresis demonstrated that the interactions between PGC-1α RID and ERR LBDs involve a single receptor subunit through high-affinity, ERR-specific L3 and low-affinity L2 interactions. NMR studies further defined the limits of PGC-1α RID that interacts with ERRs. Consistent with these findings, the solution structures of PGC-1α/ERRα LBDs and PGC-1α/ERRγ LBDs complexes share an identical architecture with an asymmetric binding of PGC-1α to homodimeric ERR.</p><p>Conclusions/Significance</p><p>These studies provide the molecular determinants for the specificity of interactions between PGC-1α and the ERRs, whereby negative cooperativity prevails in the binding of the coactivators to these receptors. Our work indicates that allosteric regulation may be a general mechanism controlling the binding of the coactivators to homodimers.</p></div>", "links"=>[], "tags"=>["Biochemistry", "proteins", "Protein interactions", "cofactors", "hormones", "biophysics", "Macromolecular assemblies", "Computational biology", "Macromolecular structure analysis", "protein structure", "Molecular cell biology", "Signal transduction", "Nuclear receptor signaling", "Endocrinology", "oncology", "Basic cancer research", "asymmetric", "binding", "receptor", "homodimers", "involves"], "article_id"=>742217, "categories"=>["Medicine", "Biological Sciences"], "users"=>["Mária Takács", "Maxim V. Petoukhov", "R. Andrew Atkinson", "Pierre Roblin", "François-Xavier Ogi", "Borries Demeler", "Noelle Potier", "Yassmine Chebaro", "Annick Dejaegere", "Dmitri I. Svergun", "Dino Moras", "Isabelle M. L. Billas"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0067810.s001", "https://dx.doi.org/10.1371/journal.pone.0067810.s002", "https://dx.doi.org/10.1371/journal.pone.0067810.s003", "https://dx.doi.org/10.1371/journal.pone.0067810.s004", "https://dx.doi.org/10.1371/journal.pone.0067810.s005", "https://dx.doi.org/10.1371/journal.pone.0067810.s006", "https://dx.doi.org/10.1371/journal.pone.0067810.s007", "https://dx.doi.org/10.1371/journal.pone.0067810.s008", "https://dx.doi.org/10.1371/journal.pone.0067810.s009", "https://dx.doi.org/10.1371/journal.pone.0067810.s010", "https://dx.doi.org/10.1371/journal.pone.0067810.s011"], "stats"=>{"downloads"=>16, "page_views"=>8, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_Asymmetric_Binding_of_PGC_1_945_to_the_ERR_945_and_ERR_947_Nuclear_Receptor_Homodimers_Involves_a_Similar_Recognition_Mechanism_/742217", "title"=>"The Asymmetric Binding of PGC-1α to the ERRα and ERRγ Nuclear Receptor Homodimers Involves a Similar Recognition Mechanism", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-07-09 02:27:38"}

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Relative Metric

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