Activity and Affinity of Pin1 Variants
1
Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO 80045, USA
2
Faculty of Pharmacy, Mansoura University, Mansoura 35516, Egypt
*
Author to whom correspondence should be addressed.
Academic Editors: Hidekazu Hiroaki and Kentaro Tomii
Molecules 2020, 25(1), 36; https://doi.org/10.3390/molecules25010036
Received: 5 November 2019
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Revised: 7 December 2019
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Accepted: 18 December 2019
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Published: 20 December 2019
(This article belongs to the Special Issue Protein Domains: Structures and Molecular Functions)
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.
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MDPI and ACS Style
Born, A.; Henen, M.A.; Vögeli, B. Activity and Affinity of Pin1 Variants. Molecules 2020, 25, 36. https://doi.org/10.3390/molecules25010036
AMA Style
Born A, Henen MA, Vögeli B. Activity and Affinity of Pin1 Variants. Molecules. 2020; 25(1):36. https://doi.org/10.3390/molecules25010036
Chicago/Turabian StyleBorn, Alexandra, Morkos A. Henen, and Beat Vögeli. 2020. "Activity and Affinity of Pin1 Variants" Molecules 25, no. 1: 36. https://doi.org/10.3390/molecules25010036
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