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Related Experiment Videos

Morpheeins--a new structural paradigm for allosteric regulation.

Eileen K Jaffe1

  • 1BioMolecular Structure and Function Group, Fox Chase Cancer Center, 333 Cottman Avenue, Philadelphia, PA 19111, USA. Eileen.Jaffe@fccc.edu

Trends in Biochemical Sciences
|July 19, 2005
PubMed
Summary

The morpheein concept reveals proteins can change quaternary structure and function. This dynamic equilibrium explains allosteric regulation and protein behavior, exemplified by porphobilinogen synthase.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Classic allosteric regulation models assume constant protein oligomeric multiplicity.
  • The morpheein concept introduces dynamic equilibria of protein structures.
  • Monomer conformation dictates quaternary structure and function.

Purpose of the Study:

  • To expand the understanding of allosteric regulation beyond static models.
  • To introduce the morpheein concept as a framework for protein dynamics.
  • To identify proteins exhibiting morpheein-like behavior.

Main Methods:

  • Conceptual framework development.
  • Analysis of protein structure-function relationships.
  • Identification of candidate proteins based on proposed morpheein dynamics.

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Main Results:

  • Porphobilinogen synthase serves as a prototype morpheein system.
  • This system involves interconverting octamer (high activity) and hexamer (low activity) isoforms.
  • Six additional candidate allosteric enzymes exhibiting morpheein behavior are proposed.

Conclusions:

  • The morpheein concept offers a novel perspective on protein allosteric regulation.
  • Dynamic monomer conformations driving quaternary structure changes are key.
  • This model enhances understanding of kinetic cooperativity and hysteresis in enzymes.