1BY1
DBL homology domain from beta-PIX
1BY1 の概要
| エントリーDOI | 10.2210/pdb1by1/pdb |
| 分子名称 | PROTEIN (PIX) (1 entity in total) |
| 機能のキーワード | rho-gtpase exchange factor, transport protein |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 23972.47 |
| 構造登録者 | Aghazadeh, B.,Zhu, K.,Kubiseski, T.J.,Liu, G.A.,Pawson, T.,Zheng, Y.,Rosen, M.K. (登録日: 1998-10-22, 公開日: 1999-10-24, 最終更新日: 2023-12-27) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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