1bwn

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spinqualitylabelsall models 1bwn, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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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