1qvi: Difference between revisions

Revision as of 16:53, 27 July 2008

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File:1qvi.png

Template:STRUCTURE 1qvi

Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the headCrystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the head

Template:ABSTRACT PUBMED 14656445

About this StructureAbout this Structure

1QVI is a Protein complex structure of sequences from Argopecten irradians. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of scallop Myosin s1 in the pre-power stroke state to 2.6 a resolution: flexibility and function in the head., Gourinath S, Himmel DM, Brown JH, Reshetnikova L, Szent-Gyorgyi AG, Cohen C, Structure. 2003 Dec;11(12):1621-7. PMID:14656445

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the head'''
+===Crystal structure of scallop myosin S1 in the pre-power stroke state to 2.6 Angstrom resolution: flexibility and function in the head===
-==Overview==
+<!--
-We have extended the X-ray structure determination of the complete scallop myosin head in the pre-power stroke state to 2.6 A resolution, allowing an atomic comparison of the three major (weak actin binding) states of various myosins. We can now account for conformational differences observed in crystal structures in the so-called "pliant region" at the motor domain-lever arm junction between scallop and vertebrate smooth muscle myosins. A hinge, which may contribute to the compliance of the myosin crossbridge, has also been identified for the first time within the regulatory light-chain domain of the lever arm. Analysis of temperature factors of key joints of the motor domain, especially the SH1 helix, provides crystallographic evidence for the existence of the "internally uncoupled" state in diverse isoforms. The agreement between structural and solution studies reinforces the view that the unwinding of the SH1 helix is a part of the cross-bridge cycle in many myosins.
+The line below this paragraph, {{ABSTRACT_PUBMED_14656445}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_14656445}}
 ==About this Structure==
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 [[Category: Pre-power stroke state]]
 [[Category: Sh1 helix]]
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