1scm
From Proteopedia
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'''STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION''' | '''STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION''' | ||
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[[Category: Cohen, C.]] | [[Category: Cohen, C.]] | ||
[[Category: Xie, X.]] | [[Category: Xie, X.]] | ||
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Revision as of 05:33, 3 May 2008
STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION
Overview
The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 A resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca(2+)-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.
About this Structure
1SCM is a Protein complex structure of sequences from Argopecten irradians. Full crystallographic information is available from OCA.
Reference
Structure of the regulatory domain of scallop myosin at 2.8 A resolution., Xie X, Harrison DH, Schlichting I, Sweet RM, Kalabokis VN, Szent-Gyorgyi AG, Cohen C, Nature. 1994 Mar 24;368(6469):306-12. PMID:8127365 Page seeded by OCA on Sat May 3 08:33:00 2008