Myomesin

From Proteopedia

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Revision as of 09:43, 12 November 2018

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spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Relevance 4 Structural highlights Function Myomesin or Skelemin is expressed in striated muscle cells. It contains type-III fibronectin (motif I) and C2-immunoglobulin (motif II) domains[1]. Myomesin is found in the M-bridges of sarcomeres which produce the muscle contraction and provide their elasticity. The giant protein Titin interconnects the major structure of sarcomeres - the M bands and Z discs. The C-terminal of titin binds to myomesin-1 and myomesin-2. Myomesin-1 and myomesin-2 have a unique N-terminal region followed by 12 motifs in the order of II-II-I-I-I-I-I-II-II-II-II-II[2]. Disease Relevance Structural highlights

3D structures of myomesin

Updated on 12-November-2018

5fm4, 5fm8 - hMyo-1 domain 4 510-618 - human
5fm5 - hMyo-1 domains 4-5 510-739 + obscurin-like-1
2y23 - hMyo-1 domains 9-11 1141-1447
2r15 - hMyo-1 domains 12-13 1225-1443
3rbs - hMyo-1 domains 10-11 1247-1447
4v10 - hMyo-1 domains 12-13 1225-1443 (mutant)
2jtd - hMyo-1 1207-1328 - NMR
2y25 - hMyo-1 domains 11-13 1357-1667

References

1. ↑ Reddy KB, Fox JE, Price MG, Kulkarni S, Gupta S, Das B, Smith DM. Nuclear localization of Myomesin-1: possible functions. J Muscle Res Cell Motil. 2008;29(1):1-8. doi: 10.1007/s10974-008-9137-x. Epub, 2008 Jun 3. PMID:18521710 doi:http://dx.doi.org/10.1007/s10974-008-9137-x
2. ↑ Schoenauer R, Bertoncini P, Machaidze G, Aebi U, Perriard JC, Hegner M, Agarkova I. Myomesin is a molecular spring with adaptable elasticity. J Mol Biol. 2005 Jun 3;349(2):367-79. doi: 10.1016/j.jmb.2005.03.055. Epub 2005, Apr 7. PMID:15890201 doi:http://dx.doi.org/10.1016/j.jmb.2005.03.055