1PBW

STRUCTURE OF BCR-HOMOLOGY (BH) DOMAIN

Summary for 1PBW

• Entry DOI: 10.2210/pdb1pbw/pdb
• Descriptor: PHOSPHATIDYLINOSITOL 3-KINASE (2 entities in total)
• Functional Keywords: phosphotransferase, tpase activating protein, gap, cdc42, phosphoinositide 3-kinase, sh3 domain, sh2 domain, signal transduction
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 48608.00

Authors

Musacchio, A.,Cantley, L.C.,Harrison, S.C. (deposition date: 1996-10-17, release date: 1997-03-12, Last modification date: 2024-02-14)

Primary citation

Musacchio, A.,Cantley, L.C.,Harrison, S.C.
Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85 alpha subunit.
Proc.Natl.Acad.Sci.USA, 93:14373-14378, 1996

PubMed Abstract: 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.

PubMed: 8962058
DOI: 10.1073/pnas.93.25.14373

Experimental method

X-RAY DIFFRACTION (2 Å)