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Aip1p Dynamics Are Altered by the R256H Mutation in Actin
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Activity and Affinity of Pin1 Variants.

Alexandra Born1, Morkos A Henen1,2, Beat Vögeli1

  • 1Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO 80045, USA.

Molecules (Basel, Switzerland)
|December 22, 2019
PubMed
Summary

Pin1, a key isomerase, undergoes functional changes via mutations. This review summarizes how altering Pin1

Keywords:
PPIase domainWW domainactivityaffinitymutantspin1

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Area of Science:

  • Biochemistry and Molecular Biology
  • Enzymology
  • Protein Structure and Function

Background:

  • Pin1 is a peptidyl-prolyl isomerase catalyzing the isomerization of phosphorylated Ser/Thr-Pro motifs.
  • Pin1 possesses two domains: a regulatory WW domain and a catalytic peptidyl-prolyl isomerase (PPIase) domain.
  • Interdomain allostery is a key feature, where ligand binding to the WW domain influences PPIase domain activity.

Purpose of the Study:

  • To comprehensively review mutations introduced in Pin1.
  • To elucidate the roles of specific interactions in Pin1's ligand binding, catalytic activity, and allosteric regulation.
  • To understand the structure-function relationships of Pin1.

Main Methods:

  • Literature review of studies involving Pin1 mutagenesis.
  • Analysis of reported functional and structural data from mutated Pin1 variants.
  • Synthesis of information on how mutations affect Pin1's interactions and activity.

Main Results:

  • Mutations have been instrumental in dissecting Pin1's ligand-binding sites and catalytic mechanisms.
  • Specific mutations reveal critical residues involved in interdomain communication and allosteric regulation.
  • Understanding these mutations provides insights into how Pin1's structure dictates its function.

Conclusions:

  • Mutational analysis is a powerful approach to understanding Pin1's complex regulation.
  • Elucidating the impact of mutations on Pin1 structure and function is crucial for drug development.
  • This review consolidates knowledge on Pin1 mutations, aiding future research in isomerase mechanisms and allostery.