This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5fm5

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:25, 6 May 2020

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

Structural highlights

5fm5 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	5fm4, 5fm8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[OBSL1_HUMAN] Defects in OBSL1 are the cause of 3M syndrome type 2 (3M2) [MIM: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.^[1]

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^[2]

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

References

↑ Hanson D, Murray PG, Sud A, Temtamy SA, Aglan M, Superti-Furga A, Holder SE, Urquhart J, Hilton E, Manson FD, Scambler P, Black GC, Clayton PE. The primordial growth disorder 3-M syndrome connects ubiquitination to the cytoskeletal adaptor OBSL1. Am J Hum Genet. 2009 Jun;84(6):801-6. doi: 10.1016/j.ajhg.2009.04.021. Epub 2009 , May 28. PMID:19481195 doi:10.1016/j.ajhg.2009.04.021
↑ 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 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of the myomesin:obscurin-like-1 complex==
-<StructureSection load='5fm5' size='340' side='right' caption='[[5fm5]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+<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. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FM5 FirstGlance]. <br>
+<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>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fm4|5fm4]], [[5fm8|5fm8]]</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=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'>[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>
 </table>
 == Disease ==
@@ Line 20: / Line 20: @@
 </div>
 <div class="pdbe-citations 5fm5" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Myomesin|Myomesin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Pernigo, S]]
 [[Category: Steiner, R A]]

5fm5

From Proteopedia

Revision as of 07:25, 6 May 2020

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

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox