1by1 | pdb_00001by1
DBL homology domain from beta-PIX
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Overview
Guanine nucleotide exchange factors in the Dbl family activate Rho GTPases, by accelerating dissociation of bound GDP, promoting acquisition of the, GTP-bound state. Dbl proteins possess a approximately 200 residue, catalytic Dbl-homology (DH) domain, that is arranged in tandem with a, C-terminal pleckstrin homology (PH) domain in nearly all cases. Here we, report the solution structure of the DH domain of human PAK-interacting, exchange protein (betaPIX). The domain is composed of 11 alpha-helices, that form a flattened, elongated bundle. The structure explains a large, body of mutagenesis data, which, along with sequence comparisons, identify, the GTPase interaction site as a surface formed by three conserved helices, near the center of one face of the domain. Proximity of the site to the DH, C-terminus suggests a means by which PH-ligand interactions may be coupled, to DH-GTPase interactions to regulate signaling through the Dbl proteins, in vivo.
About this Structure
1BY1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure and mutagenesis of the Dbl homology domain., Aghazadeh B, Zhu K, Kubiseski TJ, Liu GA, Pawson T, Zheng Y, Rosen MK, Nat Struct Biol. 1998 Dec;5(12):1098-107. PMID:9846881
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