1pbw
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(New page: 200px<br /> <applet load="1pbw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pbw, resolution 2.0Å" /> '''STRUCTURE OF BCR-HOM...)
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Revision as of 16:35, 12 November 2007
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STRUCTURE OF BCR-HOMOLOGY (BH) DOMAIN
Overview
Proteins such as the product of the break-point cluster region, chimaerin, and the Src homology 3-binding protein 3BP1, are GTPase activating, proteins (GAPs) for members of the Rho subfamily of small GTP-binding, proteins (G proteins or GTPases). A 200-residue region, named the, breakpoint cluster region-homology (BH) domain, is responsible for the GAP, activity. We describe here the crystal structure of the BH domain from the, p85 subunit of phosphatidylinositol 3-kinase at 2.0 A resolution. The, domain is composed of seven helices, having a previously unobserved, arrangement. A core of four helices contains most residues that are, conserved in the BH family. Their packing suggests the location of a, G-protein binding site. This structure of a GAP-like domain for small, GTP-binding proteins provides a framework for analyzing the function of, this class of molecules.
About this Structure
1PBW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit., Musacchio A, Cantley LC, Harrison SC, Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14373-8. PMID:8962058
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