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Missense mutations affecting a conserved cysteine pair in the TH domain of Btk

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Author

  • Mauno Vihinen
  • BF Nore
  • PT Mattsson
  • CM Backesjo
  • M Nars
  • S Koutaniemi
  • C Watanabe
  • T Lester
  • A Jones
  • HD Ochs
  • CIE Smith
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Summary, in English

Tec family protein tyrosine kinases have in their N-terminus two domains, The PH domain is followed by Tec homology (TH) domain, which consists of two motifs, The first pattern, Btk motif, is also present in some Pas GAP molecules, C-terminal half of the TH domain, a proline-rich region, has been shown to bind to SH3 domains, Mutations in Bruton's tyrosine kinase (Btk) belonging to the Tec family cause X-linked agammaglobulinemia (XLA) due to developmental arrest of B cells, Here Ive present the first missense mutations in the TH domain, The substitutions affect a conserved pair of cysteines, residues 154 and 155, involved in Zn2+ binding and thereby the mutations alter protein folding and stability. (C) 1997 Federation of European Biochemical Societies.

Publishing year

1997

Language

English

Pages

205-210

Publication/Series

FEBS Letters

Volume

413

Issue

2

Document type

Journal article

Publisher

Wiley-Blackwell

Topic

  • Biological Sciences

Keywords

  • XLA
  • kinase
  • cytoplasmic tyrosine
  • signal transduction
  • Btk
  • Bruton's tyrosine kinase
  • X-linked agammaglobulinemia
  • Ras GAP

Status

Published

ISBN/ISSN/Other

  • ISSN: 1873-3468