View source for 5fm5


==Crystal structure of the myomesin:obscurin-like-1 complex==
<StructureSection load='5fm5' size='340' side='right'caption='[[5fm5]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fm5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FM5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FM5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</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=5fm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fm5 OCA], [https://pdbe.org/5fm5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fm5 RCSB], [https://www.ebi.ac.uk/pdbsum/5fm5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fm5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYOM1_HUMAN MYOM1_HUMAN] Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent.
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== Publication Abstract from PubMed ==
The sarcomeric cytoskeleton is a network of modular proteins that integrate mechanical and signaling roles. Obscurin, or its homolog obscurin-like-1, bridges the giant ruler titin and the myosin crosslinker myomesin at the M-band. Yet, the molecular mechanisms underlying the physical obscurin(-like-1):myomesin connection, important for mechanical integrity of the M-band, remained elusive. Here, using a combination of structural, cellular, and single-molecule force spectroscopy techniques, we decode the architectural and functional determinants defining the obscurin(-like-1):myomesin complex. The crystal structure reveals a trans-complementation mechanism whereby an incomplete immunoglobulin-like domain assimilates an isoform-specific myomesin interdomain sequence. Crucially, this unconventional architecture provides mechanical stability up to forces of approximately 135 pN. A cellular competition assay in neonatal rat cardiomyocytes validates the complex and provides the rationale for the isoform specificity of the interaction. Altogether, our results reveal a novel binding strategy in sarcomere assembly, which might have implications on muscle nanomechanics and overall M-band organization.

Binding of Myomesin to Obscurin-Like-1 at the Muscle M-Band Provides a Strategy for Isoform-Specific Mechanical Protection.,Pernigo S, Fukuzawa A, Beedle AE, Holt M, Round A, Pandini A, Garcia-Manyes S, Gautel M, Steiner RA Structure. 2016 Dec 15. pii: S0969-2126(16)30357-4. doi:, 10.1016/j.str.2016.11.015. PMID:27989621<ref>PMID:27989621</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5fm5" style="background-color:#fffaf0;"></div>

==See Also==
*[[Myomesin|Myomesin]]
*[[Obscurin|Obscurin]]
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Pernigo S]]
[[Category: Steiner RA]]