Work

Activity and Affinity of Pin1 Variants

Year: 2019

Type: review

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.

Source: Molecules

DOI: 10.3390/molecules25010036

Authors: Alexandra Born, Morkos A. Henen, Beat Vögeli

Institutions: University of Colorado Anschutz, Mansoura University, University of Colorado Denver

Language: English

Topic: Signaling Pathways in Disease

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $1,824

Funder: National Institute of General Medical Sciences