1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.

Title1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.
Publication TypeJournal Article
Year of Publication2011
AuthorsHuculeci, R., L. Buts, T. Lenaerts, and N. A. J. van Nuland
JournalBiomol NMR Assign
Volume5
Issue2
Pagination181-4
Date Published2011 Oct
ISSN1874-270X
KeywordsAnimals, Antigens, Viral, Tumor, Cricetinae, Humans, Isotopes, Nuclear Magnetic Resonance, Biomolecular, Peptides, Phosphotyrosine, Protein Binding, Proto-Oncogene Proteins c-fyn, Recombinant Proteins, src Homology Domains
Abstract

SH2 domains are interaction modules uniquely dedicated to recognize phosphotyrosine sites, playing a central role in for instance the activation of tyrosine kinases or phosphatases. Here we report the (1)H, (15)N and (13)C backbone and side-chain chemical shift assignments of the SH2 domain of the human protein tyrosine kinase Fyn, both in its free state and bound to a high-affinity phosphotyrosine peptide corresponding to a specific sequence in the hamster middle-T antigen. The BMRB accession numbers are 17,368 and 17,369, respectively.

DOI10.1007/s12104-011-9295-4
Alternate JournalBiomol NMR Assign
PubMed ID21298565