View source for 6fsa


==Beta-Cardiac myosin post-rigor==
<StructureSection load='6fsa' size='340' side='right'caption='[[6fsa]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fsa]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FSA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FSA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6fsa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fsa OCA], [http://pdbe.org/6fsa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fsa RCSB], [http://www.ebi.ac.uk/pdbsum/6fsa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fsa ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/MYH7_BOVIN MYH7_BOVIN]] Muscle contraction. [[http://www.uniprot.org/uniprot/MYL3_BOVIN MYL3_BOVIN]] Regulatory light chain of myosin. Does not bind calcium. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hypertrophic cardiomyopathies (HCM) result from distinct single-point mutations in sarcomeric proteins that lead to muscle hypercontractility. While different models account for a pathological increase in the power output, clear understanding of the molecular basis of dysfunction in HCM is the mandatory next step to improve current treatments. Here, we present an optimized quasi-atomic model of the sequestered state of cardiac myosin coupled to X-ray crystallography and in silico analysis of the mechanical compliance of the lever arm, allowing the systematic study of a large set of HCM mutations and the definition of different mutation classes based on their effects on lever arm compliance, sequestered state stability, and motor functions. The present work reconciles previous models and explains how distinct HCM mutations can have disparate effects on the motor mechano-chemical parameters and yet lead to the same disease. The framework presented here can guide future investigations aiming at finding HCM treatments.

Hypertrophic cardiomyopathy disease results from disparate impairments of cardiac myosin function and auto-inhibition.,Robert-Paganin J, Auguin D, Houdusse A Nat Commun. 2018 Oct 1;9(1):4019. doi: 10.1038/s41467-018-06191-4. PMID:30275503<ref>PMID:30275503</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fsa" style="background-color:#fffaf0;"></div>

==See Also==
*[[Myosin|Myosin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Auguin, D]]
[[Category: Houdusse, A]]
[[Category: Robert-Paganin, J]]
[[Category: Hypertrophic cardiomyopathy]]
[[Category: Motor protein]]
[[Category: Myosin]]