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Activity and Affinity of Pin1 Variants
Version 1
: Received: 5 November 2019 / Approved: 6 November 2019 / Online: 6 November 2019 (02:40:49 CET)
A peer-reviewed article of this Preprint also exists.
Born, A.; Henen, M.A.; Vögeli, B. Activity and Affinity of Pin1 Variants. Molecules 2020, 25, 36. Born, A.; Henen, M.A.; Vögeli, B. Activity and Affinity of Pin1 Variants. Molecules 2020, 25, 36.
Abstract
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 activity, and interdomain allostery. Here, we summarize these mutations and their impact on Pin1’s structure and function.
Keywords
Pin1; WW domain; PPIase domain; mutants; activity; affinity
Subject
Chemistry and Materials Science, Organic Chemistry
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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