Literature DB >> 21298565

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

Radu Huculeci1, Lieven Buts, Tom Lenaerts, Nico A J van Nuland.   

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.

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Year:  2011        PMID: 21298565     DOI: 10.1007/s12104-011-9295-4

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.746


  1 in total

1.  Structural insights into the intertwined dimer of fyn SH2.

Authors:  Radu Huculeci; Abel Garcia-Pino; Lieven Buts; Tom Lenaerts; Nico van Nuland
Journal:  Protein Sci       Date:  2015-10-07       Impact factor: 6.725

  1 in total

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