2r15
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(New page: 200px<br /><applet load="2r15" size="350" color="white" frame="true" align="right" spinBox="true" caption="2r15, resolution 2.24Å" /> '''Crystal structure of...)
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Revision as of 08:59, 31 January 2008
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Crystal structure of the myomesin domains 12 and 13
Overview
Sarcomeric filament proteins display extraordinary properties in terms of, protein length and mechanical elasticity, requiring specific anchoring and, assembly mechanisms. To establish the molecular basis of terminal filament, assembly, we have selected the sarcomeric M-band protein myomesin as a, prototypic filament model. The crystal structure of the myomesin, C-terminus, comprising a tandem array of two immunoglobulin (Ig) domains, My12 and My13, reveals a dimeric end-to-end filament of 14.3 nm length., Although the two domains share the same fold, an unexpected rearrangement, of one beta-strand reveals how they are evolved into unrelated functions, terminal filament assembly (My13) and filament propagation (My12). The two, domains are connected by a six-turn alpha-helix, of which two turns are, void of any interactions with other protein parts. Thus, the overall, structure of the assembled myomesin C-terminus resembles a three-body, beads-on-the-string model with potentially elastic properties. We predict, that the found My12-helix-My13 domain topology may provide a structural, template for the filament architecture of the entire C-terminal Ig domain, array My9-My13 of myomesin.
About this Structure
2R15 is a Single protein structure of sequence from Homo sapiens with and as ligands. Known structural/functional Sites: , and . Full crystallographic information is available from OCA.
Reference
Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin., Pinotsis N, Lange S, Perriard JC, Svergun DI, Wilmanns M, EMBO J. 2008 Jan 9;27(1):253-64. Epub 2007 Dec 6. PMID:18059477
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