The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Interaction between Btk TH and SH3 domain.

På svenska

Author

Summary, in English

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.

Publishing year

2002

Language

English

Pages

325-334

Publication/Series

Biopolymers

Volume

63

Issue

5

Document type

Journal article

Publisher

John Wiley & Sons Inc.

Topic

  • Medical Genetics

Keywords

  • Plasmids: metabolism
  • Peptides: chemistry
  • Glutathione Transferase: metabolism
  • Complementary: metabolism
  • DNA
  • Escherichia coli: metabolism
  • Proline: chemistry
  • Protein-Tyrosine Kinases: chemistry
  • Recombinant Proteins: chemistry

Status

Published

ISBN/ISSN/Other

  • ISSN: 0006-3525