Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 1 (January 2007)

crystallization communications

Acta Cryst. (2007). F63, 18-20 [ doi:10.1107/S1744309106051682 ]

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

I. Gnemmi, C. Scotti, D. Cappelletti, P. L. Canonico, F. Condorelli and C. Rosano

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.

Keywords: Fes; tyrosine protein kinases.