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- Title
Activity and Affinity of Pin1 Variants.
- Authors
Born, Alexandra; Henen, Morkos A.; Vögeli, Beat; Hiroaki, Hidekazu; Tomii, Kentaro
- 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.
- Subjects
LIGAND binding (Biochemistry); PEPTIDYLPROLYL isomerase; BINDING sites; CATALYTIC activity; CATALYTIC domains; ISOMERASES
- Publication
Molecules, 2020, Vol 25, Issue 1, p36
- ISSN
1420-3049
- Publication type
Article
- DOI
10.3390/molecules25010036