A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1
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{"title"=>"A maltose-binding protein fusion construct yields a robust crystallography platform for MCL1", "type"=>"journal", "authors"=>[{"first_name"=>"Matthew C.", "last_name"=>"Clifton", "scopus_author_id"=>"7005428415"}, {"first_name"=>"David M.", "last_name"=>"Dranow", "scopus_author_id"=>"36620854000"}, {"first_name"=>"Alison", "last_name"=>"Leed", "scopus_author_id"=>"6506311436"}, {"first_name"=>"Ben", "last_name"=>"Fulroth", "scopus_author_id"=>"8340295200"}, {"first_name"=>"James W.", "last_name"=>"Fairman", "scopus_author_id"=>"12792157100"}, {"first_name"=>"Jan", "last_name"=>"Abendroth", "scopus_author_id"=>"35766303000"}, {"first_name"=>"Kateri A.", "last_name"=>"Atkins", "scopus_author_id"=>"56083209700"}, {"first_name"=>"Ellen", "last_name"=>"Wallace", "scopus_author_id"=>"56644158100"}, {"first_name"=>"Dazhong", "last_name"=>"Fan", "scopus_author_id"=>"55420461300"}, {"first_name"=>"Guoping", "last_name"=>"Xu", "scopus_author_id"=>"56643489200"}, {"first_name"=>"Z. J.", "last_name"=>"Ni", "scopus_author_id"=>"56643988400"}, {"first_name"=>"Doug", "last_name"=>"Daniels", "scopus_author_id"=>"35474285000"}, {"first_name"=>"John", "last_name"=>"Van Drie", "scopus_author_id"=>"6701925166"}, {"first_name"=>"Guo", "last_name"=>"Wei", "scopus_author_id"=>"56447730600"}, {"first_name"=>"Alex B.", "last_name"=>"Burgin", "scopus_author_id"=>"7004210430"}, {"first_name"=>"Todd R.", "last_name"=>"Golub", "scopus_author_id"=>"55892492700"}, {"first_name"=>"Brian K.", "last_name"=>"Hubbard", "scopus_author_id"=>"22961591000"}, {"first_name"=>"Michael H.", "last_name"=>"Serrano-Wu", "scopus_author_id"=>"6603079918"}], "year"=>2015, "source"=>"PLoS ONE", "identifiers"=>{"isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "pmid"=>"25909780", "doi"=>"10.1371/journal.pone.0125010", "pui"=>"604371989", "issn"=>"19326203", "sgr"=>"84929379135", "scopus"=>"2-s2.0-84929379135"}, "id"=>"52cdc5d7-f5a4-346f-9742-bf1dd02404e0", "abstract"=>"Crystallization of a maltose-binding protein MCL1 fusion has yielded a robust crystallography platform that generated the first apo MCL1 crystal structure, as well as five ligand-bound structures. The ability to obtain fragment-bound structures advances structure-based drug design efforts that, despite considerable effort, had previously been intractable by crystallography. In the ligand-independent crystal form we identify inhibitor binding modes not observed in earlier crystallographic systems. This MBP-MCL1 construct dramatically improves the structural understanding of well-validated MCL1 ligands, and will likely catalyze the structure-based optimization of high affinity MCL1 inhibitors.", "link"=>"http://www.mendeley.com/research/maltosebinding-protein-fusion-construct-yields-robust-crystallography-platform-mcl1", "reader_count"=>30, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Professor > Associate Professor"=>1, "Researcher"=>11, "Student > Ph. D. Student"=>8, "Student > Postgraduate"=>1, "Other"=>2, "Student > Master"=>3, "Lecturer"=>2, "Lecturer > Senior Lecturer"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Professor > Associate Professor"=>1, "Researcher"=>11, "Student > Ph. D. Student"=>8, "Student > Postgraduate"=>1, "Other"=>2, "Student > Master"=>3, "Lecturer"=>2, "Lecturer > Senior Lecturer"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>8, "Agricultural and Biological Sciences"=>9, "Medicine and Dentistry"=>2, "Design"=>1, "Pharmacology, Toxicology and Pharmaceutical Science"=>2, "Chemistry"=>7}, "reader_count_by_subdiscipline"=>{"Design"=>{"Design"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>2}, "Chemistry"=>{"Chemistry"=>7}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>9}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>8}, "Unspecified"=>{"Unspecified"=>1}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>2}}, "reader_count_by_country"=>{"Uruguay"=>1, "United States"=>2, "United Kingdom"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/2038754"], "description"=>"<p>The structure of MBP-MCL1 with ligand <b>2</b> (yellow) determined to 1.55 Å (blue) overlaid with the structure of MCL1 171–323 determined at 2.4 Å (PDB ID 4HW2, gray).</p>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393581, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0125010.g005", "stats"=>{"downloads"=>1, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Comparison_of_PDB_4HW2_and_MBP_MCL1_with_ligand_2_/1393581", "title"=>"Comparison of PDB 4HW2 and MBP-MCL1 with ligand 2.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-04-24 02:48:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/2038767"], "description"=>"<p>Fragment <b>5</b> (yellow) binds similarly in comparison to the elaborated ligand from PDB ID 4OQ6 (gray).</p>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393594, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0125010.g007", "stats"=>{"downloads"=>5, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_structure_of_MBP_MCL1_bound_to_fragment_5_determined_at_1_9_197_/1393594", "title"=>"The structure of MBP-MCL1 bound to fragment 5 determined at 1.9 Å.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-04-24 02:48:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/2038749"], "description"=>"<p>(A) The structure of MCL1 173–321 was determined to 1.70 Å. (B) In the ligand-bound MCL1 173–321 structure, the imidazole group of <b>1</b> coordinates with zinc along with H224 and pyrophosphate.</p>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393576, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0125010.g002", "stats"=>{"downloads"=>5, "page_views"=>24, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Crystal_packing_of_MCL1_173_8211_321_is_mediated_by_zinc_and_pyrophosphate_/1393576", "title"=>"Crystal packing of MCL1 173–321 is mediated by zinc and pyrophosphate.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-04-24 02:48:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/2038747"], "description"=>"<p>MCL1 ligands used in co-crystallization experiments.</p>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393574, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0125010.g001", "stats"=>{"downloads"=>1, "page_views"=>14, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MCL1_ligands_used_in_co_crystallization_experiments_/1393574", "title"=>"MCL1 ligands used in co-crystallization experiments.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-04-24 02:48:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/2038758"], "description"=>"<p>The structure of MBP-MCL1 with fragment <b>4</b> (yellow) determined to 2.4 Å (blue) overlaid with the structure of MCL1 171–323 determined at 2.4 Å (PDB ID 4HW3, gray). The carboxylic acid of 4HW3 adopts multiple conformations depending on the chain; only chain A is shown for clarity.</p>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393585, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0125010.g006", "stats"=>{"downloads"=>3, "page_views"=>17, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Comparison_of_PDB_4HW3_and_MBP_MCL1_with_fragment_4_/1393585", "title"=>"Comparison of PDB 4HW3 and MBP-MCL1 with fragment 4.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-04-24 02:48:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/2038770"], "description"=>"<p>(A) The surface side-view shows that fragment <b>6</b> shifts and makes water mediated hydrogen bond contacts with the peptide backbone of R263. (B) The elaborated ligand of fragment <b>6</b> (PDB ID 4OQ5) shifts to allow the methyl-naphthalene to bind in the hydrophobic pocket, requiring the carboxylic acid to make a single hydrogen bond with the sidechain of R263. (C) Overlay of crystallized fragment <b>6</b> and the elaborated ligand in PDB ID 4OQ5 reveals a distinct binding pose for <b>6</b>.</p>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393597, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0125010.g008", "stats"=>{"downloads"=>2, "page_views"=>16, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structure_of_MBP_MCL1_bound_to_fragment_6_determined_at_2_0_197_/1393597", "title"=>"Structure of MBP-MCL1 bound to fragment 6 determined at 2.0 Å.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-04-24 02:48:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/2038752"], "description"=>"<p>In the absence of zinc and pyrophosphate, the pyridine ring of <b>1</b> rotates 180° away from H224 allowing the imidazole to face out towards the solvent channel.</p>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393579, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0125010.g004", "stats"=>{"downloads"=>0, "page_views"=>21, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Removal_of_crystal_packing_interactions_allows_sidechain_rotation_of_ligand_1_/1393579", "title"=>"Removal of crystal packing interactions allows sidechain rotation of ligand 1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-04-24 02:48:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/2038751"], "description"=>"<p>(A) The MBP domain (red) is connected by a short GS linker (orange) to MCL1 173–321 (blue). A portion of alpha helix four is not ordered in the structure (red dashed-line). Maltose ligand is shown in yellow. (B) The MCL1 domain is structurally very similar to the NMR structure of Apo-MCL1 (gray).</p>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393578, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0125010.g003", "stats"=>{"downloads"=>1, "page_views"=>29, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_structure_of_Apo_MBP_MCL1_determined_at_1_90_197_/1393578", "title"=>"The structure of Apo MBP-MCL1 determined at 1.90 Å.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-04-24 02:48:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/2038782", "https://ndownloader.figshare.com/files/2038783", "https://ndownloader.figshare.com/files/2038784", "https://ndownloader.figshare.com/files/2038785"], "description"=>"<div><p>Crystallization of a maltose-binding protein MCL1 fusion has yielded a robust crystallography platform that generated the first apo MCL1 crystal structure, as well as five ligand-bound structures. The ability to obtain fragment-bound structures advances structure-based drug design efforts that, despite considerable effort, had previously been intractable by crystallography. In the ligand-independent crystal form we identify inhibitor binding modes not observed in earlier crystallographic systems. This MBP-MCL1 construct dramatically improves the structural understanding of well-validated MCL1 ligands, and will likely catalyze the structure-based optimization of high affinity MCL1 inhibitors.</p></div>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393608, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0125010.s001", "https://dx.doi.org/10.1371/journal.pone.0125010.s002", "https://dx.doi.org/10.1371/journal.pone.0125010.s003", "https://dx.doi.org/10.1371/journal.pone.0125010.s004"], "stats"=>{"downloads"=>21, "page_views"=>34, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_A_Maltose_Binding_Protein_Fusion_Construct_Yields_a_Robust_Crystallography_Platform_for_MCL1_/1393608", "title"=>"A Maltose-Binding Protein Fusion Construct Yields a Robust Crystallography Platform for MCL1", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2015-04-24 02:48:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/2038777"], "description"=>"<p>Surface representations are shown as side views and ligands are shown as yellow sticks. (A and B) Fragment 4 maps onto L78 of NoxaB from PDB ID 2NLA, with only minor structural perturbation of the BH3-binding groove of MCL1. In contrast, binding of fragment 6 creates a significant pocket (C) which is further expanded upon binding of ligand 1 (D).</p>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393604, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0125010.g009", "stats"=>{"downloads"=>1, "page_views"=>28, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_conformational_flexibility_of_the_binding_pocket_of_MCL1_/1393604", "title"=>"The conformational flexibility of the binding pocket of MCL1.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-04-24 02:48:18"}
  • {"files"=>["https://ndownloader.figshare.com/files/2038780"], "description"=>"<p>All experiments are n ≥ 3, and averaged values for K<sub>D</sub> are reported.</p><p>Binding affinity (K<sub>D</sub>) of ligands to MCL1 and MBP-MCL1.</p>", "links"=>[], "tags"=>["inhibitor binding modes", "affinity MCL 1 inhibitors", "crystallography platform", "effort", "MCL 1 Crystallization", "apo MCL 1 crystal structure", "Robust Crystallography Platform"], "article_id"=>1393606, "categories"=>["Biological Sciences"], "users"=>["Matthew C. Clifton", "David M. Dranow", "Alison Leed", "Ben Fulroth", "James W. Fairman", "Jan Abendroth", "Kateri A. Atkins", "Ellen Wallace", "Dazhong Fan", "Guoping Xu", "Z. J. Ni", "Doug Daniels", "John Van Drie", "Guo Wei", "Alex B. Burgin", "Todd R. Golub", "Brian K. Hubbard", "Michael H. Serrano-Wu"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0125010.t001", "stats"=>{"downloads"=>3, "page_views"=>34, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Binding_affinity_K_D_of_ligands_to_MCL1_and_MBP_MCL1_/1393606", "title"=>"Binding affinity (K<sub>D</sub>) of ligands to MCL1 and MBP-MCL1.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2015-04-24 02:48:18"}

PMC Usage Stats | Further Information

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Relative Metric

{"start_date"=>"2015-01-01T00:00:00Z", "end_date"=>"2015-12-31T00:00:00Z", "subject_areas"=>[]}

F1000Prime | Further Information

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