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5fm5

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Crystal structure of the myomesin:obscurin-like-1 complex

Structural highlights

5fm5 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYOM1_HUMAN Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5fm5"

Categories: Homo sapiens | Large Structures | Pernigo S | Steiner RA

@@ Line 3: / Line 3: @@
 <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 [http://en.wikipedia.org/wiki/Human Human]. 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 [http://proteopedia.org/fgij/fg.htm?mol=5FM5 FirstGlance]. <br>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fm4|5fm4]], [[5fm8|5fm8]]</td></tr>
+</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'>[http://proteopedia.org/fgij/fg.htm?mol=5fm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fm5 OCA], [http://pdbe.org/5fm5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fm5 RCSB], [http://www.ebi.ac.uk/pdbsum/5fm5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fm5 ProSAT]</span></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>
-== Disease ==
-[[http://www.uniprot.org/uniprot/OBSL1_HUMAN OBSL1_HUMAN]] Defects in OBSL1 are the cause of 3M syndrome type 2 (3M2) [MIM:[http://omim.org/entry/612921 612921]]. An autosomal recessive disorder characterized by severe pre- and postnatal growth retardation, facial dysmorphism, large head circumference, and normal intelligence and endocrine function. Skeletal changes include long slender tubular bones and tall vertebral bodies.<ref>PMID:19481195</ref>
 == Function ==
-[[http://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.
+[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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 21: @@
 ==See Also==
 *[[Myomesin|Myomesin]]
+*[[Obscurin|Obscurin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Pernigo, S]]
+[[Category: Pernigo S]]
-[[Category: Steiner, R A]]
+[[Category: Steiner RA]]
-[[Category: Cytoskeletal protein]]
-[[Category: Fibronectin domain]]
-[[Category: Immunoglobulin-like domain]]
-[[Category: M-band]]
-[[Category: Protein complex]]
-[[Category: Sarcomere]]
-[[Category: Structural protein]]

5fm5

From Proteopedia

Current revision

Crystal structure of the myomesin:obscurin-like-1 complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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