The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop

T. V. Borchert, M. Mathieu, J. Ph Zeelen, S. A. Courtneidge, R. K. Wierenga

Research output: Contribution to journalArticle

59 Scopus citations

Abstract

SH3 domains are modules occurring in diverse proteins, ranging from cytoskeletal proteins to signaling proteins, such as tyrosine kinases. The crystal structure of the SH3 domain of Csk (c-Src specific tyrosine kinase) has been refined at a resolution of 2.5 Å, with an R-factor of 22.4%. The structure is very similar to the FynSHS crystal structure. When comparing CskSHS and FynSH3 it is seen that the structural and charge differences of the RT-Src loop and the n-Src loop, near the conserved Trp47, correlate with different binding properties of these SH3 domains. The structure comparison suggests that those glycines and acid residues which are very well conserved in the SH3 sequences are important for the stability of the SH3 fold.

Original languageEnglish (US)
Pages (from-to)79-85
Number of pages7
JournalFEBS Letters
Volume341
Issue number1
DOIs
StatePublished - Mar 14 1994

Keywords

  • Averaging
  • Crystal structure
  • Csk
  • Fyn
  • Src
  • Tyrosine kinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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