1pbw

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1pbw, resolution 2.00Å ()
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Contents

STRUCTURE OF BCR-HOMOLOGY (BH) DOMAIN

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1pbw is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Musacchio A, Cantley LC, Harrison SC. Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit. Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14373-8. PMID:8962058
  • Sandelin E. On hydrophobicity and conformational specificity in proteins. Biophys J. 2004 Jan;86(1 Pt 1):23-30. PMID:14695246 doi:10.1016/S0006-3495(04)74080-1

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