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Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.

par Huculeci, Radu;Buts, Lieven;Lenaerts, Tom ;van Nuland, Nico A J;Garcia-Pino, Abel
Référence Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 68, Pt 3, page (359-364)
Publication Publié, 2012-03

Article révisé par les pairs

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Résumé :

SH2 domains are widespread protein-binding modules that recognize phosphotyrosines and play central roles in intracellular signalling pathways. The SH2 domain of the human protein tyrosine kinase Fyn has been expressed, purified and crystallized in the unbound state and in complex with a high-affinity phosphotyrosine peptide. X-ray data were collected to a resolution of 2.00 Å for the unbound form and 1.40 Å for the protein in complex with the phosphotyrosine peptide.