2ix7

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[[Image:2ix7.gif|left|200px]]
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{{STRUCTURE_2ix7| PDB=2ix7 | SCENE= }}
{{STRUCTURE_2ix7| PDB=2ix7 | SCENE= }}
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'''STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V'''
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===STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17151196 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17151196}}
==About this Structure==
==About this Structure==
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[[Category: Phosphorylation]]
[[Category: Phosphorylation]]
[[Category: Ubl conjugation]]
[[Category: Ubl conjugation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:01:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:45:34 2008''

Revision as of 09:45, 28 July 2008

Template:STRUCTURE 2ix7

STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V

Template:ABSTRACT PUBMED 17151196

About this Structure

2IX7 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

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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