Structural Basis for Specificity of Propeptide-Enzyme Interaction in Barley C1A Cysteine Peptidases
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{"title"=>"Structural basis for specificity of propeptide-enzyme interaction in barley C1A cysteine peptidases", "type"=>"journal", "authors"=>[{"first_name"=>"Inés", "last_name"=>"Cambra", "scopus_author_id"=>"34978262500"}, {"first_name"=>"David", "last_name"=>"Hernández", "scopus_author_id"=>"57197605611"}, {"first_name"=>"Isabel", "last_name"=>"Diaz", "scopus_author_id"=>"56510288900"}, {"first_name"=>"Manuel", "last_name"=>"Martinez", "scopus_author_id"=>"35463373800"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "scopus"=>"2-s2.0-84861208629", "sgr"=>"84861208629", "pui"=>"364837546", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "pmid"=>"22615948", "doi"=>"10.1371/journal.pone.0037234"}, "id"=>"cedee230-666e-3199-bb39-ee14916a0bff", "abstract"=>"C1A cysteine peptidases are synthesized as inactive proenzymes. Activation takes place by proteolysis cleaving off the inhibitory propeptide. The inhibitory capacity of propeptides from barley cathepsin L and B-like peptidases towards commercial and barley cathepsins has been characterized. Differences in selectivity have been found for propeptides from L-cathepsins against their cognate and non cognate enzymes. Besides, the propeptide from barley cathepsin B was not able to inhibit bovine cathepsin B. Modelling of their three-dimensional structures suggests that most propeptide inhibitory properties can be explained from the interaction between the propeptide and the mature cathepsin structures. Their potential use as biotechnological tools is discussed.", "link"=>"http://www.mendeley.com/research/structural-basis-specificity-propeptideenzyme-interaction-barley-c1a-cysteine-peptidases", "reader_count"=>17, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>6, "Student > Ph. D. Student"=>6, "Student > Master"=>3, "Student > Bachelor"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>6, "Student > Ph. D. Student"=>6, "Student > Master"=>3, "Student > Bachelor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>3, "Agricultural and Biological Sciences"=>10, "Medicine and Dentistry"=>3, "Physics and Astronomy"=>1}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>3}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>10}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}}, "reader_count_by_country"=>{"Uruguay"=>1, "France"=>1}, "group_count"=>0}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/636751"], "description"=>"<p>(a) Homology models of barley cathepsin L-like peptidases created using SWISS-MODEL. The propeptides (green) and their corresponding mature enzymes (blue; catalytic triad residues in red) are shown. (b) Alignment of the amino acid regions of the propeptides from barley L cathepsins. Alignment was generated using the MUSCLE program. The location of residues belonging to the conserved ERFNIN and GNFD motifs (red and green boxes), and the position of a variable key amino acid putatively involved in the interaction propeptide-HvPap-10 enzyme (orange box) are indicated. (c) Ribbon plots showing the structural overlay of three-dimensional models for propeptides from HvPap-4 (green), HvPap-6 (orange), HvPap-10 (blue) and HvPap-16 (purple) peptidases and their interaction with the homology model for HvPap-10 (red). Amino acid residues in position 99 (HvPap-10 numbering) are depicted in stick mode. Close-up image shows the molecular surface of K277 of HvPap-10 peptidase, which is potentially involved in a steric clash with the side chain of H108 of the HvPap-16pro.</p>", "links"=>[], "tags"=>["barley", "l-like"], "article_id"=>307248, "categories"=>["Biochemistry", "Biotechnology", "Biological Sciences"], "users"=>["Inés Cambra", "David Hernandez", "Isabel Diaz", "Manuel Martinez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0037234.g003", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structure_sequence_analysis_of_barley_L_like_cathepsins_/307248", "title"=>"Structure-sequence analysis of barley L-like cathepsins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 02:00:48"}
  • {"files"=>["https://ndownloader.figshare.com/files/637019"], "description"=>"<p>ni, no inhibitory activity observed at 5 µM concentration of the propeptide.</p>", "links"=>[], "tags"=>["constants", "barley", "propeptides", "cathepsin", "l-like", "c1a", "cysteine"], "article_id"=>307504, "categories"=>["Biochemistry", "Biotechnology", "Biological Sciences"], "users"=>["Inés Cambra", "David Hernandez", "Isabel Diaz", "Manuel Martinez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0037234.t001", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Inhibition_constants_K_i_values_of_the_barley_propeptides_HvPap_4pro_6pro_10pro_16pro_19pro_against_barley_cathepsin_L_like_HvPap_4_6_10_16_and_commercial_cathepsin_B_BovCathB_C1A_cysteine_peptidases_/307504", "title"=>"Inhibition constants (<i>K</i><sub>i</sub>) values of the barley propeptides (HvPap-4pro, -6pro, -10pro, -16pro, -19pro) against barley cathepsin L-like (HvPap-4, -6, -10, -16) and commercial cathepsin B (BovCathB) C1A cysteine peptidases.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-05-17 02:05:04"}
  • {"files"=>["https://ndownloader.figshare.com/files/328872", "https://ndownloader.figshare.com/files/328973"], "description"=>"<div><p>C1A cysteine peptidases are synthesized as inactive proenzymes. Activation takes place by proteolysis cleaving off the inhibitory propeptide. The inhibitory capacity of propeptides from barley cathepsin L and B-like peptidases towards commercial and barley cathepsins has been characterized. Differences in selectivity have been found for propeptides from L-cathepsins against their cognate and non cognate enzymes. Besides, the propeptide from barley cathepsin B was not able to inhibit bovine cathepsin B. Modelling of their three-dimensional structures suggests that most propeptide inhibitory properties can be explained from the interaction between the propeptide and the mature cathepsin structures. Their potential use as biotechnological tools is discussed.</p> </div>", "links"=>[], "tags"=>["specificity", "propeptide-enzyme", "barley", "c1a", "cysteine", "peptidases"], "article_id"=>124946, "categories"=>["Biochemistry", "Biotechnology", "Biological Sciences"], "users"=>["Inés Cambra", "David Hernandez", "Isabel Diaz", "Manuel Martinez"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0037234.s001", "https://dx.doi.org/10.1371/journal.pone.0037234.s002"], "stats"=>{"downloads"=>2, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Structural_Basis_for_Specificity_of_Propeptide_Enzyme_Interaction_in_Barley_C1A_Cysteine_Peptidases/124946", "title"=>"Structural Basis for Specificity of Propeptide-Enzyme Interaction in Barley C1A Cysteine Peptidases", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-05-17 01:22:26"}
  • {"files"=>["https://ndownloader.figshare.com/files/636480"], "description"=>"<p>A. Purification of the recombinant HvPap propeptides from <i>E. coli</i> cultures by SDS-PAGE. Five µg of each protein were loaded. Five µg of an extract of pRSETB without insert were used as a control of protein purity. The gel was stained with Coomassie Brillant Blue G. M: molecular markers (KD). <b>B</b>. Example of Lineweaver-Burk plot. HvPap-10 competitive inhibition in the presence of HvPap-4pro. Water was used as a control.</p>", "links"=>[], "tags"=>["inhibitory"], "article_id"=>306975, "categories"=>["Biochemistry", "Biotechnology", "Biological Sciences"], "users"=>["Inés Cambra", "David Hernandez", "Isabel Diaz", "Manuel Martinez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0037234.g001", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Purification_and_inhibitory_mechanism_of_propeptides_/306975", "title"=>"Purification and inhibitory mechanism of propeptides.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 01:56:15"}
  • {"files"=>["https://ndownloader.figshare.com/files/636589"], "description"=>"<p>(a) Homology models of bovine and barley HvPap-19 cathepsin B peptidases created using SWISS-MODEL. The propeptides (green) and the mature enzymes (blue; catalytic triad residues in red) are shown. Arrows mark the occluding loop domains. (b) Alignment of the amino acid regions involved in the interaction between the occluding loop and the propeptide in different animal and plant species. Alignment was generated using the MUSCLE program. The locations of residues potentially involved in steric clashes (red boxes) are indicated. Pp, <i>Physcomitrella patens</i>; Sm, <i>Selaginella moellendorffii</i>; Os, <i>Oryza sativa</i>; Hv, <i>Hordeum vulgare</i>; Pt, <i>Populus trichocarpa</i>; At, <i>Arabidopsis thaliana</i>. (c) Ribbon plots showing the structural overlay of three-dimensional models for bovine cathepsin B (orange) and HvPap-19 (green). Close-up image shows the molecular surface of V174 located in the occluding loop of bovine cathepsin B and Y59 in the propeptide of HvPap-19, which are potentially involved in a steric clash.</p>", "links"=>[], "tags"=>["biotechnology", "Computational biology", "Biochemistry"], "article_id"=>307085, "categories"=>["Biochemistry", "Biotechnology", "Biological Sciences"], "users"=>["Inés Cambra", "David Hernandez", "Isabel Diaz", "Manuel Martinez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0037234.g002", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structure_sequence_analysis_of_animal_and_plant_B_cathepsins_/307085", "title"=>"Structure-sequence analysis of animal and plant B cathepsins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 01:58:05"}
  • {"files"=>["https://ndownloader.figshare.com/files/636924"], "description"=>"<p>Ribbon plots show the structural overlay of the propeptide sequences from HvPap-19 (red) and the barley L-cathepsins (green). Mature peptidases of barley L-cathepsins (HvPap-4, -6, -10 and -16) are coloured in blue.</p>", "links"=>[], "tags"=>["models", "cathepsin", "hvpap-19", "propeptide", "barley", "l-like"], "article_id"=>307407, "categories"=>["Biochemistry", "Biotechnology", "Biological Sciences"], "users"=>["Inés Cambra", "David Hernandez", "Isabel Diaz", "Manuel Martinez"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0037234.g004", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Homology_models_showing_the_interaction_of_the_cathepsin_B_HvPap_19_propeptide_with_barley_L_like_cathepsins_/307407", "title"=>"Homology models showing the interaction of the cathepsin B HvPap-19 propeptide with barley L-like cathepsins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-05-17 02:03:27"}

PMC Usage Stats | Further Information

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Relative Metric

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