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Intermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase

Hansson, H; Okoh, MP; Smith, CIE; Vihinen, Mauno LU and Hard, T (2001) In FEBS Letters 489(1). p.67-70
Abstract
The SH3 domain of Bruton's tyrosine kinase (Btk) is preceded by the Tec homology (TH) region containing proline-rich sequences. We have studied a protein fragment containing both the Btk SH3 domain and the proline-rich sequences of the TH region (PRR-SH3). Intermolecular NMR cross-relaxation measurements, gel permeation chromatography profiles, titrations with proline-rich peptides, and N-15 NMR relaxation measurements are all consistent with a monomer-dimer equilibrium with a dissociation constant on the order of 60 muM. The intermolecular interactions do, at least in part, involve proline-rich sequences in the TH region. This behavior of Btk PRR-SH3 may have implications for the functional action of Btk. (C) 2001 Federation of European... (More)
The SH3 domain of Bruton's tyrosine kinase (Btk) is preceded by the Tec homology (TH) region containing proline-rich sequences. We have studied a protein fragment containing both the Btk SH3 domain and the proline-rich sequences of the TH region (PRR-SH3). Intermolecular NMR cross-relaxation measurements, gel permeation chromatography profiles, titrations with proline-rich peptides, and N-15 NMR relaxation measurements are all consistent with a monomer-dimer equilibrium with a dissociation constant on the order of 60 muM. The intermolecular interactions do, at least in part, involve proline-rich sequences in the TH region. This behavior of Btk PRR-SH3 may have implications for the functional action of Btk. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Bruton's tyrosine kinase, Src homology 3, dimerization, nuclear magnetic, resonance, gel permeation chromatography, signal transduction
in
FEBS Letters
volume
489
issue
1
pages
67 - 70
publisher
Wiley-Blackwell
external identifiers
  • wos:000166730000014
  • scopus:0035951350
ISSN
1873-3468
DOI
10.1016/S0014-5793(00)02438-8
language
English
LU publication?
no
id
20542d69-2d47-4730-b28d-739393961299 (old id 3851694)
date added to LUP
2013-06-28 15:25:42
date last changed
2018-02-18 04:24:39
@article{20542d69-2d47-4730-b28d-739393961299,
  abstract     = {The SH3 domain of Bruton's tyrosine kinase (Btk) is preceded by the Tec homology (TH) region containing proline-rich sequences. We have studied a protein fragment containing both the Btk SH3 domain and the proline-rich sequences of the TH region (PRR-SH3). Intermolecular NMR cross-relaxation measurements, gel permeation chromatography profiles, titrations with proline-rich peptides, and N-15 NMR relaxation measurements are all consistent with a monomer-dimer equilibrium with a dissociation constant on the order of 60 muM. The intermolecular interactions do, at least in part, involve proline-rich sequences in the TH region. This behavior of Btk PRR-SH3 may have implications for the functional action of Btk. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.},
  author       = {Hansson, H and Okoh, MP and Smith, CIE and Vihinen, Mauno and Hard, T},
  issn         = {1873-3468},
  keyword      = {Bruton's tyrosine kinase,Src homology 3,dimerization,nuclear magnetic,resonance,gel permeation chromatography,signal transduction},
  language     = {eng},
  number       = {1},
  pages        = {67--70},
  publisher    = {Wiley-Blackwell},
  series       = {FEBS Letters},
  title        = {Intermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase},
  url          = {http://dx.doi.org/10.1016/S0014-5793(00)02438-8},
  volume       = {489},
  year         = {2001},
}