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Interaction between Btk TH and SH3 domain.

Okoh, Michael P and Vihinen, Mauno LU (2002) In Biopolymers 63(5). p.325-334
Abstract
Several mechanisms are involved in the regulation of cellular signaling. Bruton tyrosine kinase (Btk) of the Tec family contains in the Tec homology (TH) domain a proline-rich region (PRR) capable of interacting with several SH3 domains. The Btk has the SH3 domain adjacent to the TH domain. CD and fluorescence spectroscopy were used to study the binding of two peptides corresponding to segments in the PRR to the Btk SH3 domain. The peptide for the N-terminal half of the PRR binds specifically, whereas the other peptide had hardly any affinity. The TH domain has about four times lower affinity to the SH3 domain than the peptide, 17.0 vs 3.9 microM. The interaction was further tested with an SH3 domain construct that contained the PRR. The... (More)
Several mechanisms are involved in the regulation of cellular signaling. Bruton tyrosine kinase (Btk) of the Tec family contains in the Tec homology (TH) domain a proline-rich region (PRR) capable of interacting with several SH3 domains. The Btk has the SH3 domain adjacent to the TH domain. CD and fluorescence spectroscopy were used to study the binding of two peptides corresponding to segments in the PRR to the Btk SH3 domain. The peptide for the N-terminal half of the PRR binds specifically, whereas the other peptide had hardly any affinity. The TH domain has about four times lower affinity to the SH3 domain than the peptide, 17.0 vs 3.9 microM. The interaction was further tested with an SH3 domain construct that contained the PRR. The two peptides cannot compete for the binding to the extended protein and the TH domain has two times lower affinity to the extended SH3 domain. The intra- or intermolecular interaction between the TH and SH3 domain might have regulatory function also in the other Tec family members. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Plasmids: metabolism, Peptides: chemistry, Glutathione Transferase: metabolism, Complementary: metabolism, DNA, Escherichia coli: metabolism, Proline: chemistry, Protein-Tyrosine Kinases: chemistry, Recombinant Proteins: chemistry
in
Biopolymers
volume
63
issue
5
pages
325 - 334
publisher
John Wiley & Sons
external identifiers
  • pmid:11877742
  • scopus:0037092006
ISSN
0006-3525
DOI
10.1002/bip.10049
language
English
LU publication?
no
id
6b0ef681-cd7d-4a28-a853-85c8a033eb6e (old id 3635613)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/11877742?dopt=Abstract
date added to LUP
2013-06-12 16:01:54
date last changed
2017-01-01 07:39:38
@article{6b0ef681-cd7d-4a28-a853-85c8a033eb6e,
  abstract     = {Several mechanisms are involved in the regulation of cellular signaling. Bruton tyrosine kinase (Btk) of the Tec family contains in the Tec homology (TH) domain a proline-rich region (PRR) capable of interacting with several SH3 domains. The Btk has the SH3 domain adjacent to the TH domain. CD and fluorescence spectroscopy were used to study the binding of two peptides corresponding to segments in the PRR to the Btk SH3 domain. The peptide for the N-terminal half of the PRR binds specifically, whereas the other peptide had hardly any affinity. The TH domain has about four times lower affinity to the SH3 domain than the peptide, 17.0 vs 3.9 microM. The interaction was further tested with an SH3 domain construct that contained the PRR. The two peptides cannot compete for the binding to the extended protein and the TH domain has two times lower affinity to the extended SH3 domain. The intra- or intermolecular interaction between the TH and SH3 domain might have regulatory function also in the other Tec family members.},
  author       = {Okoh, Michael P and Vihinen, Mauno},
  issn         = {0006-3525},
  keyword      = {Plasmids: metabolism,Peptides: chemistry,Glutathione Transferase: metabolism,Complementary: metabolism,DNA,Escherichia coli: metabolism,Proline: chemistry,Protein-Tyrosine Kinases: chemistry,Recombinant Proteins: chemistry},
  language     = {eng},
  number       = {5},
  pages        = {325--334},
  publisher    = {John Wiley & Sons},
  series       = {Biopolymers},
  title        = {Interaction between Btk TH and SH3 domain.},
  url          = {http://dx.doi.org/10.1002/bip.10049},
  volume       = {63},
  year         = {2002},
}