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

Vihinen, Mauno LU ; Nore, BF; Mattsson, PT; Backesjo, CM; Nars, M; Koutaniemi, S; Watanabe, C; Lester, T; Jones, A and Ochs, HD, et al. (1997) In FEBS Letters 413(2). p.205-210
Abstract
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... (More)
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. (Less)
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type
Contribution to journal
publication status
published
subject
keywords
XLA, kinase, cytoplasmic tyrosine, signal transduction, Btk, Bruton's tyrosine kinase, X-linked agammaglobulinemia, Ras GAP
in
FEBS Letters
volume
413
issue
2
pages
205 - 210
publisher
Wiley-Blackwell
external identifiers
  • wos:A1997XT08500005
  • scopus:17144437356
ISSN
1873-3468
DOI
10.1016/S0014-5793(97)00912-5
language
English
LU publication?
no
id
93f48b8e-3aa9-4d2a-beaa-20c3a0222242 (old id 3852810)
date added to LUP
2013-06-28 14:32:10
date last changed
2017-01-01 06:53:27
@article{93f48b8e-3aa9-4d2a-beaa-20c3a0222242,
  abstract     = {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.},
  author       = {Vihinen, Mauno and Nore, BF and Mattsson, PT and Backesjo, CM and Nars, M and Koutaniemi, S and Watanabe, C and Lester, T and Jones, A and Ochs, HD and Smith, CIE},
  issn         = {1873-3468},
  keyword      = {XLA,kinase,cytoplasmic tyrosine,signal transduction,Btk,Bruton's tyrosine kinase,X-linked agammaglobulinemia,Ras GAP},
  language     = {eng},
  number       = {2},
  pages        = {205--210},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {Missense mutations affecting a conserved cysteine pair in the TH domain of Btk},
  url          = {http://dx.doi.org/10.1016/S0014-5793(97)00912-5},
  volume       = {413},
  year         = {1997},
}