Missense mutations affecting a conserved cysteine pair in the TH domain of Btk
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3852810
- author
- publishing date
- 1997
- 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
- 2016-04-01 16:01:16
- date last changed
- 2022-01-28 08:44:21
@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}}, keywords = {{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}}, doi = {{10.1016/S0014-5793(97)00912-5}}, volume = {{413}}, year = {{1997}}, }