Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

@article{Jacobs2003PeptideBI,
  title={Peptide binding induces large scale changes in inter-domain mobility in human Pin1.},
  author={Doris M. Jacobs and Krishna G. Saxena and Martin Vogtherr and Pau Bernad{\'o} and Miquel Pons and Klaus M. Fiebig},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 28},
  pages={
          26174-82
        }
}
Pin1 is a peptidyl-prolyl cis/trans isomerase (PPIase) essential for cell cycle regulation. Pin1-catalyzed peptidyl-prolyl isomerization provides a key conformational switch to activate phosphorylation sites with the common phospho-Ser/Thr-Pro sequence motif. This motif is ubiquitously exploited in cellular response to a variety of signals. Pin1 is able to bind phospho-Ser/Thr-Pro-containing sequences at two different sites that compete for the same substrate. One binding site is located within… CONTINUE READING
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