5k6p

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(New page: '''Unreleased structure''' The entry 5k6p is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (10:12, 14 June 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5k6p is ON HOLD
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==The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C==
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<StructureSection load='5k6p' size='340' side='right'caption='[[5k6p]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5k6p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K6P FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5k6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k6p OCA], [https://pdbe.org/5k6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k6p RCSB], [https://www.ebi.ac.uk/pdbsum/5k6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k6p ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/MYPC3_HUMAN MYPC3_HUMAN] Defects in MYBPC3 are the cause of familial hypertrophic cardiomyopathy type 4 (CMH4) [MIM:[https://omim.org/entry/115197 115197]. Familial hypertrophic cardiomyopathy is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.<ref>PMID:7744002</ref> <ref>PMID:9048664</ref> <ref>PMID:9562578</ref> <ref>PMID:9541104</ref> <ref>PMID:9541115</ref> <ref>PMID:11499718</ref> <ref>PMID:11499719</ref> <ref>PMID:12379228</ref> <ref>PMID:11815426</ref> <ref>PMID:12951062</ref> <ref>PMID:12707239</ref> <ref>PMID:12974739</ref> <ref>PMID:14563344</ref> <ref>PMID:12628722</ref> <ref>PMID:12818575</ref> <ref>PMID:15114369</ref> <ref>PMID:15519027</ref> <ref>PMID:15563892</ref> <ref>PMID:16199542</ref> <ref>PMID:18403758</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/MYPC3_HUMAN MYPC3_HUMAN] Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The nuclear magnetic resonance (NMR) structure of the tri-helix bundle (THB) of the m-domain plus C2 (DeltamC2) of myosin-binding protein C (MyBP-C) has revealed a highly flexible seven-residue linker between the structured THB and C2. Bioinformatics shows significant patterns of conservation across the THB-linker sequence, with the linker containing a strictly conserved serine in all MyBP-C isoforms. Clinically linked mutations further support the functional significance of the THB-linker region. NMR, small-angle X-ray scattering, and binding studies show the THB-linker plus the first ten residues of C2 undergo dramatic changes when DeltamC2 binds Ca2+-calmodulin, with the linker and C2 N-terminal residues contributing significantly to the affinity. Modeling of all available experimental data indicates that the THB tertiary structure must be disrupted to form the complex. These results are discussed in the context of the THB-linker and the N-terminal residues of C2 forming a polymorphic binding domain that could accommodate multiple binding partners in the dynamic sarcomere.
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Authors:
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A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C.,Michie KA, Kwan AH, Tung CS, Guss JM, Trewhella J Structure. 2016 Nov 1;24(11):2000-2007. doi: 10.1016/j.str.2016.08.018. Epub 2016, Oct 6. PMID:27720588<ref>PMID:27720588</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5k6p" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Guss JM]]
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[[Category: Kwan AH]]
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[[Category: Michie KA]]
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[[Category: Trewhella J]]
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[[Category: Tung CS]]

Current revision

The NMR structure of the m domain tri-helix bundle and C2 of human cardiac Myosin Binding Protein C

PDB ID 5k6p

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