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

TitlePurification, crystallization and preliminary X-ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.
Publication TypeJournal Article
Year of Publication2012
AuthorsHuculeci, R., L. Buts, T. Lenaerts, N. A. J. van Nuland, and A. Garcia-Pino
JournalActa Crystallogr Sect F Struct Biol Cryst Commun
Volume68
IssuePt 3
Pagination359-64
Date Published2012 Mar 1
ISSN1744-3091
KeywordsCrystallization, Crystallography, X-Ray, Humans, Peptides, Phosphotyrosine, Proto-Oncogene Proteins c-fyn, src Homology Domains
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.

DOI10.1107/S1744309112004186
Alternate JournalActa Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
PubMed ID22442244
PubMed Central IDPMC3310552