1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide |
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| Authors: | Radu Huculeci Lieven Buts Tom Lenaerts Nico A J van Nuland |
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| Institution: | (1) Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussel, Belgium;(2) Department of Molecular and Cellular Interactions, VIB, Pleinlaan 2, 1050 Brussel, Belgium;(3) MLG, D?partement d’informatique, Universit? Libre de Bruxelles, Boulevard du Triomphe CP212, 1050 Brussel, Belgium;(4) AI-lab, Vakgroep Computerwetenschappen, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussel, Belgium; |
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| 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 1H, 15N and 13C 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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