Activity and Affinity of Pin1 Variants.
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ABSTRACT:
SUBMITTER: Born A
PROVIDER: S-EPMC6983177 | biostudies-literature | 2019 Dec
REPOSITORIES: biostudies-literature
Publications
Activity and Affinity of Pin1 Variants.
Born Alexandra A Henen Morkos A MA Vögeli Beat B
Molecules (Basel, Switzerland) 20191220 1
Pin1 is a peptidyl-prolyl isomerase responsible for isomerizing phosphorylated S/T-P motifs. Pin1 has two domains that each have a distinct ligand binding site, but only its PPIase domain has catalytic activity. Vast evidence supports interdomain allostery of Pin1, with binding of a ligand to its regulatory WW domain impacting activity in the PPIase domain. Many diverse studies have made mutations in Pin1 in order to elucidate interactions that are responsible for ligand binding, isomerase activ ...[more]
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