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.
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This research is funded by the Flemish Scientific Fund (F.W.O.) via the grant G025915N. The VIB and the Jean Jeener NMR Center provided further support for our work.
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In Memoriam Nico van Nuland.
We would like to dedicate this article to the memory of our colleague and friend Nico van Nuland who passed away on November 4, 2017, without whom this research would not have been possible.
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Kieken, F., Loth, K., van Nuland, N. et al. Chemical shift assignments of the partially deuterated Fyn SH2–SH3 domain. Biomol NMR Assign 12, 117–122 (2018). https://doi.org/10.1007/s12104-017-9792-1
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DOI: https://doi.org/10.1007/s12104-017-9792-1