Intermolecular interactions between the SH3 domain and the proline-rich TH region of Bruton's tyrosine kinase
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3851694
- author
- Hansson, H ; Okoh, MP ; Smith, CIE ; Vihinen, Mauno LU and Hard, T
- publishing date
- 2001
- 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
- 2016-04-01 16:09:58
- date last changed
- 2022-01-28 17:44:36
@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}}, keywords = {{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}}, doi = {{10.1016/S0014-5793(00)02438-8}}, volume = {{489}}, year = {{2001}}, }