1by1
From Proteopedia
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[[Image:1by1.gif|left|200px]] | [[Image:1by1.gif|left|200px]] | ||
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'''DBL homology domain from beta-PIX''' | '''DBL homology domain from beta-PIX''' | ||
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[[Category: Zheng, Y.]] | [[Category: Zheng, Y.]] | ||
[[Category: Zhu, K.]] | [[Category: Zhu, K.]] | ||
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Revision as of 09:06, 2 May 2008
DBL homology domain from beta-PIX
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 Page seeded by OCA on Fri May 2 12:06:03 2008
