Preprint Review Version 1 This version is not peer-reviewed

Activity and Affinity of Pin1 Variants

Version 1 : Received: 5 November 2019 / Approved: 6 November 2019 / Online: 6 November 2019 (02:40:49 CET)

How to cite: Born, A.; Henen, M.A.; Vögeli, B. Activity and Affinity of Pin1 Variants. Preprints 2019, 2019110050 (doi: 10.20944/preprints201911.0050.v1). Born, A.; Henen, M.A.; Vögeli, B. Activity and Affinity of Pin1 Variants. Preprints 2019, 2019110050 (doi: 10.20944/preprints201911.0050.v1).

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.

Subject Areas

Pin1; WW domain; PPIase domain; mutants; activity; affinity

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