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Chemical shift assignments of the partially deuterated Fyn SH2–SH3 domain

par Kieken, Fabien;Loth, Karine;van Nuland, Nico N.A.J.;Tompa, Peter;Lenaerts, Tom
Référence Biomolecular N M R Assignments, 12, 1, page (117-122)
Publication Publié, 2018-04

Article révisé par les pairs

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Résumé :

Src Homology 2 and 3 (SH2 and SH3) are two key protein interaction modules involved in regulating the activity of many proteins such as tyrosine kinases and phosphatases by respective recognition of phosphotyrosine and proline-rich regions. In the Src family kinases, the inactive state of the protein is the direct result of the interaction of the SH2 and the SH3 domain with intra-molecular regions, leading to a closed structure incompetent with substrate modification. Here, we report the 1H, 15N and 13C backbone- and side-chain chemical shift assignments of the partially deuterated Fyn SH3–SH2 domain and structural differences between tandem and single domains. The BMRB accession number is 27165.