Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of the Fyn SH2 domain and its complex with a phosphotyrosine peptide
Author(s) -
Huculeci Radu,
Buts Lieven,
Lenaerts Tom,
van Nuland Nico A. J.,
GarciaPino Abel
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112004186
Subject(s) - sh2 domain , fyn , peptide , phosphopeptide , proto oncogene tyrosine protein kinase src , tyrosine kinase , sh3 domain , biochemistry , chemistry , microbiology and biotechnology , biophysics , biology , phosphorylation , signal transduction
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.