1BY1
DBL homology domain from beta-PIX
Summary for 1BY1
| Entry DOI | 10.2210/pdb1by1/pdb |
| Descriptor | PROTEIN (PIX) (1 entity in total) |
| Functional Keywords | rho-gtpase exchange factor, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 23972.47 |
| Authors | Aghazadeh, B.,Zhu, K.,Kubiseski, T.J.,Liu, G.A.,Pawson, T.,Zheng, Y.,Rosen, M.K. (deposition date: 1998-10-22, release date: 1999-10-24, Last modification date: 2023-12-27) |
| Primary citation | Aghazadeh, B.,Zhu, K.,Kubiseski, T.J.,Liu, G.A.,Pawson, T.,Zheng, Y.,Rosen, M.K. Structure and Mutagenesis of the Dbl Homology Domain Nat.Struct.Biol., 5:1098-1107, 1998 Cited by PubMed Abstract: 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. PubMed: 9846881DOI: 10.1038/4209 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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