Title | Chemical shift assignments of the partially deuterated Fyn SH2-SH3 domain. |
Publication Type | Journal Article |
Year of Publication | 2018 |
Authors | Kieken, F., K. Loth, N. van Nuland, P. Tompa, and T. Lenaerts |
Journal | Biomol NMR Assign |
Volume | 12 |
Issue | 1 |
Pagination | 117-122 |
Date Published | 2018 Apr |
ISSN | 1874-270X |
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. |
DOI | 10.1007/s12104-017-9792-1 |
Alternate Journal | Biomol NMR Assign |
PubMed ID | 29224116 |
Grant List | G025915N / / Fonds Wetenschappelijk Onderzoek / |
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