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

Risultato della ricerca: Contributo su rivistaArticolo in rivistapeer 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.

Lingua originaleInglese
pagine (da-a)18-20
Numero di pagine3
RivistaActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Numero di pubblicazione1
DOI
Stato di pubblicazionePubblicato - gen 2007

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