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

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. 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.