Pin1 two-state structural ensembles of apo, FFpSPR-bound and pCDC25c-bound form

<p>Pin1 is a two-domain cell regulator that isomerizes peptidyl-prolines. The catalytic domain (PPIase) and the other ligand-binding domain (WW) sample extended and compact conformations. Ligand binding changes the equilibrium of the interdomain conformations through an interdomain allosteric mechanism. We have described ligand-specific conformational changes that occur upon binding of pCDC25c and FFpSPR. pCDC25c binding doubles the population of the extended states compared to the virtually identical populations of the apo and FFpSPR-bound forms. pCDC25c binding to the WW domain triggers conformational changes to propagate via the interdomain interface to the catalytic site, while FFpSPR binding displaces a helix in the PPIase that leads to repositioning of the PPIase catalytic loop.</p> <p>Here, we deposit the entire magnetic resonance-based CYANA structure calculation protocols of Pin1 two-state structural ensembles of apo, FFpSPR-bound and pCDC25c-bound form that allowed us to determine the coupling of intra- and interdomain structural sampling Pin1.</p>