Chemical shift assignments of the partially deuterated Fyn SH2-SH3 domain.

TitleChemical shift assignments of the partially deuterated Fyn SH2-SH3 domain.
Publication TypeJournal Article
Year of Publication2018
AuthorsKieken, F., K. Loth, N. van Nuland, P. Tompa, and T. Lenaerts
JournalBiomol NMR Assign
Volume12
Issue1
Pagination117-122
Date Published2018 Apr
ISSN1874-270X
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 H, N and C 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.

DOI10.1007/s12104-017-9792-1
Alternate JournalBiomol NMR Assign
PubMed ID29224116
Grant ListG025915N / / Fonds Wetenschappelijk Onderzoek /
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