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Related Experiment Videos

Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

Doris M Jacobs1, Krishna Saxena, Martin Vogtherr

  • 1Institut für Organische Chemie und Chemische Biologie, Johann Wolfgang Goethe-Universität Frankfurt, Marie-Curie Strasse 11, 60439 Frankfurt, Germany. d.jacobs@nmr.uni-frankfurt.de

The Journal of Biological Chemistry
|April 11, 2003
PubMed
Summary

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Pin1, a key enzyme in cell cycle regulation, dynamically adjusts its structure based on bound peptides. This flexibility influences how Pin1 interacts with its targets, impacting cellular signaling pathways.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Pin1 is a peptidyl-prolyl cis/trans isomerase (PPIase) crucial for cell cycle regulation.
  • It recognizes and isomerizes phospho-Ser/Thr-Pro motifs, activating downstream signaling.
  • Pin1 possesses two distinct binding sites within its WW and catalytic domains.

Purpose of the Study:

  • To elucidate the solution structure and dynamics of full-length Pin1.
  • To investigate how target peptides influence inter-domain interactions within Pin1.

Main Methods:

  • High-resolution Nuclear Magnetic Resonance (NMR) spectroscopy.
  • 15N spin relaxation measurements.
  • Differential chemical shift mapping and residual dipolar coupling analysis.

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Main Results:

  • Pin1 exhibits dynamic inter-domain interactions, behaving as either independent domains or a single unit with hinge motion.
  • The flexibility is modulated by the specific sequence of the bound peptide.
  • NMR data reveal distinct conformational states influenced by peptide binding.

Conclusions:

  • Pin1's domain flexibility is adaptable and regulated by its substrates.
  • This dynamic regulation is critical for Pin1's diverse roles in cellular signaling.
  • Understanding Pin1's conformational plasticity is key to its function in various cellular processes.