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

Kieken, Fabien and Loth, Karine and van Nuland, Nico and Tompa, Péter and Lenaerts, Tom (2018) Chemical shift assignments of the partially deuterated Fyn SH2–SH3 domain. BIOMOLECULAR NMR ASSIGNMENTS, 12 (1). pp. 117-122. ISSN 1874-2718

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Abstract

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. © 2017, Springer Science+Business Media B.V., part of Springer Nature.

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