1scm

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{{STRUCTURE_1scm| PDB=1scm | SCENE= }}
{{STRUCTURE_1scm| PDB=1scm | SCENE= }}
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'''STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION'''
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===STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8127365 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8127365}}
==About this Structure==
==About this Structure==
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[[Category: Xie, X.]]
[[Category: Xie, X.]]
[[Category: Calcium-binding protein]]
[[Category: Calcium-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:57:20 2008''

Revision as of 10:57, 28 July 2008

Template:STRUCTURE 1scm

STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8127365

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

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