1bwn

From Proteopedia

Revision as of 09:00, 30 October 2007

PH DOMAIN AND BTK MOTIF FROM BRUTON'S TYROSINE KINASE MUTANT E41K IN COMPLEX WITH INS(1,3,4,5)P4

Overview

BACKGROUND: The activity of Bruton's tyrosine kinase (Btk) is important, for the maturation of B cells. A variety of point mutations in this enzyme, result in a severe human immunodeficiency known as X-linked, agammaglobulinemia (XLA). Btk contains a pleckstrin-homology (PH) domain, that specifically binds phosphatidylinositol 3,4,5-trisphosphate and, hence, responds to signalling via phosphatidylinositol 3-kinase. Point, mutations in the PH domain might abolish membrane binding, preventing, signalling via Btk. RESULTS: We have determined the crystal structures of, the wild-type PH domain and a gain-of-function mutant E41K in complex with, D-myo-inositol 1,3,4,5-tetra-kisphosphate (Ins (1,3,4,5)P4). The inositol, Ins (1,3,4,5)P4 binds to a site that is similar to the inositol, ... [(full description)]

About this Structure

1BWN is a [Single protein] structure of sequence from [Homo sapiens] with ZN and 4IP as [ligands]. Active as [Transferred entry: 2.7.10.1 and 2.7.10.2], with EC number [2.7.1.112]. Structure known Active Sites: ZN1 and ZN2. Full crystallographic information is available from [OCA].

Reference

Structure of the PH domain from Bruton's tyrosine kinase in complex with inositol 1,3,4,5-tetrakisphosphate., Baraldi E, Carugo KD, Hyvonen M, Surdo PL, Riley AM, Potter BV, O'Brien R, Ladbury JE, Saraste M, Structure. 1999 Apr 15;7(4):449-60. PMID:10196129

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