|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5fm5' size='340' side='right'caption='[[5fm5]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='5fm5' size='340' side='right'caption='[[5fm5]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == 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]] 3.1Å</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> | | </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 == | | == 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 21: |
| | ==See Also== | | ==See Also== |
| | *[[Myomesin|Myomesin]] | | *[[Myomesin|Myomesin]] |
| | + | *[[Obscurin|Obscurin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[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]]
| + | |
| Structural highlights
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.
See Also
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
|
