title: Purification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.
abstract: 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.
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels, Belgium.
authors.forename: Radu
authors.initials: R
authors.lastname: Huculeci
authors.forename: Lieven
authors.initials: L
authors.lastname: Buts
authors.forename: Tom
authors.initials: T
authors.lastname: Lenaerts
authors.forename: Nico A J
authors.initials: NA
authors.lastname: van Nuland
authors.forename: Abel
authors.initials: A
authors.lastname: Garcia-Pino
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D010455:Peptides / Q000737:chemistry*; D019000:Phosphotyrosine / Q000737:chemistry*; D051076:Proto-Oncogene Proteins c-fyn / Q000737:chemistry* / Q000302:isolation & purification; D018909:src Homology Domains
chemical_list: D010455:Peptides; D019000:Phosphotyrosine; C494957:FYN protein, human; D051076:Proto-Oncogene Proteins c-fyn