2ix7

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Revision as of 20:53, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2ix7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ix7, resolution 2.50Å" /> '''STRUCTURE OF APO-CA...)
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File:2ix7.gif


2ix7, resolution 2.50Å

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STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V

OverviewOverview

A 2.5-A resolution structure of calcium-free calmodulin (CaM) bound to the, first two IQ motifs of the murine myosin V heavy chain reveals an unusual, CaM conformation. The C-terminal lobe of each CaM adopts a semi-open, conformation that grips the first part of the IQ motif (IQxxxR), whereas, the N-terminal lobe adopts a closed conformation that interacts more, weakly with the second part of the motif (GxxxR). Variable residues in the, IQ motif play a critical role in determining the precise structure of the, bound CaM, such that even the consensus residues of different motifs show, unique interactions with CaM. This complex serves as a model for the lever, arm region of many classes of unconventional myosins, as well as other IQ, motif-containing proteins such as neuromodulin and IQGAPs.

About this StructureAbout this Structure

2IX7 is a [Protein complex] structure of sequences from [Mus musculus] with SO4 and CYS as [ligands]. Full crystallographic information is available from [OCA].

ReferenceReference

Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features., Houdusse A, Gaucher JF, Krementsova E, Mui S, Trybus KM, Cohen C, Proc Natl Acad Sci U S A. 2006 Dec 19;103(51):19326-31. Epub 2006 Dec 6. PMID:17151196

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