Abstract
Pin1 is a human peptidyl-prolyl cis–trans isomerase important for the regulation of phosphoproteins that are implicated in many diseases including cancer and Alzheimer’s. Further biophysical study of Pin1 will elucidate the importance of the two-domain system to regulate its own activity. Here, we report near-complete backbone and side-chain 1H, 13C and 15N NMR chemical shift assignments of full-length, apo Pin1 for the purpose of studying interdomain allostery and dynamics.
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Acknowledgements
We would like to thank Dr. David Jones at University of Colorado for helping set up initial experiments. This work was supported by a start-up package from the University of Colorado at Denver to B.V.
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Born, A., Nichols, P.J., Henen, M.A. et al. Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery. Biomol NMR Assign 13, 85–89 (2019). https://doi.org/10.1007/s12104-018-9857-9
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DOI: https://doi.org/10.1007/s12104-018-9857-9