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Related Experiment Video

Updated: May 8, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Published on: March 3, 2015

Interdomain interactions support interdomain communication in human Pin1.

Kimberly A Wilson¹, Jill J Bouchard, Jeffrey W Peng

¹Department of Chemistry and Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.

|September 12, 2013

Summary

This summary is machine-generated.

Pin1, a mitotic regulator, uses interdomain communication for activity. Weakening contacts in a Pin1 mutant (I28A) altered its function and flexibility, supporting allosteric communication via interdomain interactions.

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Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Pin1 is a crucial mitotic regulator comprising a peptidyl-prolyl isomerase (PPIase) domain and a Trp-Trp (WW) binding domain.
Interdomain communication is vital for Pin1's in vivo function, but its atomic underpinnings are not fully understood.
Previous studies suggested weak interdomain contacts facilitate allosteric communication between the domain interface and the PPIase active site.

Purpose of the Study:

To investigate the sensitivity of Pin1's PPIase domain to interdomain contact.
To elucidate the atomic basis of allosteric communication in Pin1.
To test the hypothesis that interdomain contacts support allosteric communication.

Main Methods:

Generation of a Pin1 mutant (I28A) to weaken interdomain contact while preserving domain structures.
Utilized Nuclear Magnetic Resonance (NMR) spectroscopy to study Pin1 functional dynamics.
Assessed substrate binding affinity and isomerase activity of the wild-type and mutant Pin1.

Main Results:

The I28A mutation altered substrate binding affinity and isomerase activity.
Long-range perturbations in conformational flexibility were observed in both domains of the I28A mutant.
These changes occurred in both apo and substrate-bound states, indicating sensitivity to interdomain contact.

Conclusions:

The PPIase domain's conformational flexibility is sensitive to interdomain contact.
The findings strengthen the hypothesis that interdomain contacts mediate allosteric communication in Pin1.
This mechanism of interdomain interaction may be applicable to other modular biological systems.