Expression, purification and preliminary crystallographic studies on the catalytic region of the nonreceptor tyrosine kinase Fes

Ilaria Gnemmi, Claudia Scotti, Donata Cappelletti, Pier Luigi Canonico, Fabrizio Condorelli, Camillo Rosano

Research output: Contribution to journalArticlepeer-review

Abstract

The proto-oncogene tyrosine protein kinase c-fps/fes encodes a structurally unique protein (Fes) of the nonreceptor protein-tyrosine kinase (PTK) family. Its expression has been demonstrated in myeloid haematopoietic cells, vascular endothelial cells and in neurons. In human-derived and murine-derived cell lines, the activated form of this kinase can induce cellular transformation; moreover, it has been shown that Fes is involved in the regulation of cell-cell and cell-matrix interactions mediated by adherens junctions and focal adhesions. The N-terminus of Fes contains the FCH (Fps/Fes/Fer/CIP4 homology) domain, which is unique to the Fes/Fer kinase family. It is followed by three coiled-coil domains and an SH2 (Src-homology 2) domain. The catalytic region (Fes-CR) is located at the C-terminus of the protein. The successful expression, purification and crystallization of the catalytic part of Fes (Fes-CR) are described.

Original languageEnglish
Pages (from-to)18-20
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number1
DOIs
Publication statusPublished - Jan 2007

Keywords

  • Fes
  • Tyrosine protein kinases

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

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