1btk | pdb_00001btk
PH DOMAIN AND BTK MOTIF FROM BRUTON'S TYROSINE KINASE MUTANT R28C
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Overview
Bruton's tyrosine kinase (Btk) is an enzyme which is involved in, maturation of B cells. It is a target for mutations causing X-linked, agammaglobulinaemia (XLA) in man. We have determined the structure of the, N-terminal part of Btk by X-ray crystallography at 1.6 A resolution. This, part of the kinase contains a pleckstrin homology (PH) domain and a Btk, motif. The structure of the PH domain is similar to those published, previously: a seven-stranded bent beta-sheet with a C-terminal, alpha-helix. Individual point mutations within the Btk PH domain which, cause XLA can be classified as either structural or functional in the, light of the three-dimensional structure and biochemical data. All, functional mutations cluster into the positively charged end of the, molecule around the ... [(full description)]
About this Structure
1BTK is a [Single protein] structure of sequence from [Homo sapiens] with ZN and NA 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 and Btk motif from Bruton's tyrosine kinase: molecular explanations for X-linked agammaglobulinaemia., Hyvonen M, Saraste M, EMBO J. 1997 Jun 16;16(12):3396-404. PMID:9218782
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