2esw
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(New page: 200px<br /><applet load="2esw" size="450" color="white" frame="true" align="right" spinBox="true" caption="2esw, resolution 2.01Å" /> '''Atomic structure of ...)
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Revision as of 08:00, 21 November 2007
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Atomic structure of the N-terminal SH3 domain of mouse beta PIX,p21-activated kinase (PAK)-interacting exchange factor
Overview
The mouse betaPIX-SH3 domain, residues 8-63 of P21-activated kinase, interacting exchange factor, has been characterized by X-ray diffraction., Crystals belonging to space group P3(2)21 diffracted to 2.0 A and the, structure was phased by the single-wavelength anomalous diffraction, method. The domain is a compact beta-barrel with an overall conformation, similar to the general SH3 structure. The X-ray structure shows mouse, betaPIX-SH3 domain binding the way in which the betaPIX characteristic, amino acids do so for an unconventional ligand binding surface. This, arrangement provides a rationale for the unusual ligand recognition motif, exhibited by mouse betaPIX-SH3 domain. Comparison with another SH3/peptide, complex shows that the recognition mode of the mouse betaPIX-SH3 domain, should be very similar to the RXXK ligand binding mode. The unique large, and planar hydrophobic pocket may contribute to the promiscuity of, betaPIX-SH3 domain resulting in its multiple biological functions.
About this Structure
2ESW is a Single protein structure of sequence from Mus musculus with HG and CL as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the N-terminal SH3 domain of mouse betaPIX, p21-activated kinase-interacting exchange factor., Li X, Liu X, Sun F, Gao J, Zhou H, Gao GF, Bartlam M, Rao Z, Biochem Biophys Res Commun. 2006 Jan 6;339(1):407-14. Epub 2005 Nov 14. PMID:16307729
Page seeded by OCA on Wed Nov 21 10:07:30 2007
Categories: Mus musculus | Single protein | Rao, Z. | CL | HG | Beta barrel | Sh3 domain
