Expression, purification and preliminary crystallographic studies on the catalytic region of the nonreceptor tyrosine kinase Fes
- DiSCAFF&DFB Center, Università del Piemonte Orientale ‘A. Avogadro’, Via Giovanni Bovio 6, 28100, Novara (Italy)
- Dipartimento di Medicina Sperimentale, Sezione di Patologia Generale, Università di Pavia, Piazza Botta 10, 27100 Pavia (Italy)
- National Institute for Cancer Research (IST), Largo R. Benzi 10, 16132 Genova (Italy)
The catalytic domain of human Fes tyrosine kinase has been cloned, expressed, purified and crystallized. 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.
- OSTI ID:
- 22360242
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 1 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
Similar Records
Chromosomal localization of the mouse Src-like adapter protein (Slap) gene and its putative human homolog SLA
Molecular cloning, characterization, and chromosomal localization of a human lymphoid tyrosine kinase related to murine Blk