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

Abstract

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.

Authors:
 [1]; ;  [2]; ;  [1];  [3];  [4]
  1. DiSCAFF&DFB Center, Università del Piemonte Orientale ‘A. Avogadro’, Via Giovanni Bovio 6, 28100, Novara (Italy)
  2. Dipartimento di Medicina Sperimentale, Sezione di Patologia Generale, Università di Pavia, Piazza Botta 10, 27100 Pavia (Italy)
  3. National Institute for Cancer Research (IST), Largo R. Benzi 10, 16132 Genova (Italy)
  4. (Italy)
Publication Date:
OSTI Identifier:
22360242
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 1; Other Information: PMCID: PMC2330100; PMID: 17183165; PUBLISHER-ID: bw5170; OAI: oai:pubmedcentral.nih.gov:2330100; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; INTERACTIONS; IRON SULFIDES; TRANSFORMATIONS

Citation Formats

Gnemmi, Ilaria, Scotti, Claudia, Cappelletti, Donata, Canonico, Pier Luigi, Condorelli, Fabrizio, Rosano, Camillo, E-mail: camillo.rosano@istge.it, and DiSCAFF&DFB Center, Università del Piemonte Orientale ‘A. Avogadro’, Via Giovanni Bovio 6, 28100, Novara. Expression, purification and preliminary crystallographic studies on the catalytic region of the nonreceptor tyrosine kinase Fes. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309106051682.
Gnemmi, Ilaria, Scotti, Claudia, Cappelletti, Donata, Canonico, Pier Luigi, Condorelli, Fabrizio, Rosano, Camillo, E-mail: camillo.rosano@istge.it, & DiSCAFF&DFB Center, Università del Piemonte Orientale ‘A. Avogadro’, Via Giovanni Bovio 6, 28100, Novara. Expression, purification and preliminary crystallographic studies on the catalytic region of the nonreceptor tyrosine kinase Fes. United Kingdom. doi:10.1107/S1744309106051682.
Gnemmi, Ilaria, Scotti, Claudia, Cappelletti, Donata, Canonico, Pier Luigi, Condorelli, Fabrizio, Rosano, Camillo, E-mail: camillo.rosano@istge.it, and DiSCAFF&DFB Center, Università del Piemonte Orientale ‘A. Avogadro’, Via Giovanni Bovio 6, 28100, Novara. Mon . "Expression, purification and preliminary crystallographic studies on the catalytic region of the nonreceptor tyrosine kinase Fes". United Kingdom. doi:10.1107/S1744309106051682.
@article{osti_22360242,
title = {Expression, purification and preliminary crystallographic studies on the catalytic region of the nonreceptor tyrosine kinase Fes},
author = {Gnemmi, Ilaria and Scotti, Claudia and Cappelletti, Donata and Canonico, Pier Luigi and Condorelli, Fabrizio and Rosano, Camillo, E-mail: camillo.rosano@istge.it and DiSCAFF&DFB Center, Università del Piemonte Orientale ‘A. Avogadro’, Via Giovanni Bovio 6, 28100, Novara},
abstractNote = {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.},
doi = {10.1107/S1744309106051682},
journal = {Acta Crystallographica. Section F},
number = Pt 1,
volume = 63,
place = {United Kingdom},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}