|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|
|Date Published||2018 Apr|
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.
|Alternate Journal||Biomol NMR Assign|
|Grant List||G025915N / / Fonds Wetenschappelijk Onderzoek /|
Chemical shift assignments of the partially deuterated Fyn SH2-SH3 domain.