1scm

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(New page: 200px<br /><applet load="1scm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1scm, resolution 2.8&Aring;" /> '''STRUCTURE OF THE REGU...)
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[[Image:1scm.gif|left|200px]]<br /><applet load="1scm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1scm, resolution 2.8&Aring;" />
caption="1scm, resolution 2.8&Aring;" />
'''STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION'''<br />
'''STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION'''<br />
==Overview==
==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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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==
==About this Structure==
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1SCM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SCM OCA].
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1SCM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Argopecten_irradians Argopecten irradians] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCM OCA].
==Reference==
==Reference==
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[[Category: calcium-binding protein]]
[[Category: calcium-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:16:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:00:11 2008''

Revision as of 13:00, 21 February 2008


1scm, resolution 2.8Å

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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 with as ligand. 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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