Interaction between Btk TH and SH3 domain.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3635613
- author
- Okoh, Michael P and Vihinen, Mauno LU
- publishing date
- 2002
- 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 Inc.
- external identifiers
-
- pmid:11877742
- scopus:0037092006
- pmid:11877742
- 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
- 2016-04-04 08:54:08
- date last changed
- 2022-01-29 07:28:07
@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}}, keywords = {{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 Inc.}}, series = {{Biopolymers}}, title = {{Interaction between Btk TH and SH3 domain.}}, url = {{http://dx.doi.org/10.1002/bip.10049}}, doi = {{10.1002/bip.10049}}, volume = {{63}}, year = {{2002}}, }