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TitleConformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering.
Journal, issue, pagesEMBO J, Vol. 22, Issue 18, Page 4616-4624, Year 2003
Publish dateSep 15, 2003
AuthorsJosé A Márquez / C I Edvard Smith / Maxim V Petoukhov / Paola Lo Surdo / Pekka T Mattsson / Marika Knekt / Anna Westlund / Klaus Scheffzek / Matti Saraste / Dmitri I Svergun /
PubMed AbstractBrutons's tyrosine kinase (Btk) is a non-receptor protein tyrosine kinase (nrPTK) essential for the development of B lymphocytes in humans and mice. Like Src and Abl PTKs, Btk contains a conserved ...Brutons's tyrosine kinase (Btk) is a non-receptor protein tyrosine kinase (nrPTK) essential for the development of B lymphocytes in humans and mice. Like Src and Abl PTKs, Btk contains a conserved cassette formed by SH3, SH2 and protein kinase domains, but differs from them by the presence of an N-terminal PH domain and the Tec homology region. The domain structure of Btk was analysed using X-ray synchrotron radiation scattering in solution. Low resolution shapes of the full-length protein and several deletion mutants determined ab initio from the scattering data indicated a linear arrangement of domains. This arrangement was further confirmed by rigid body modelling using known high resolution structures of individual domains. The final model of Btk displays an extended conformation with no, or little, inter-domain interactions. In agreement with these results, deletion of non-catalytic domains failed to enhance the activity of Btk. Taken together, our results indicate that, contrary to Src and Abl, Btk might not require an assembled conformation for the regulation of its activity.
External linksEMBO J / PubMed:12970174 / PubMed Central
MethodsSAS (X-ray synchrotron)
Structure data

SASDC52:
Bruton tyrosine kinase (Tyrosine-protein kinase BTK (R28C mutant), BTK)
Method: SAXS/SANS

Source
  • Homo sapiens (human)

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