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

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.
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Submitted on : Friday, December 29, 2017 - 5:20:31 PM
Last modification on : Tuesday, November 12, 2019 - 2:36:03 PM

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Fabien Kieken, Karine Loth, Nico van Nuland, Peter Tompa, Tom Lenaerts. Chemical shift assignments of the partially deuterated Fyn SH2–SH3 domain. Biomolecular NMR Assignments, Springer, 2017, ⟨10.1007/s12104-017-9792-1⟩. ⟨hal-01673443⟩

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