2ix7

File:2ix7.gif

spinqualitylabelsall models 2ix7, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V

Overview

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 Structure

2IX7 is a Protein complex structure of sequences from Mus musculus with SO4 and CYS as ligands. Structure known Active Site: AC1. 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

Page seeded by OCA on Mon Nov 5 14:21:28 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA