Mechanisms of cooperativity and allosteric regulation in proteins

1989/05/01 by M. F. Perutz · 3 citations
Biochemistry, Genetics and Molecular Biology · Medicine · #Hemoglobin structure and function #Protein Structure and Dynamics #Erythrocyte Function and Pathophysiology

paper · doi:10.1017/s0033583500003826

Abstract

AUosteric proteins control and coordinate chemical events in the living cell. When Monod conceived that idea he said that he had discovered the second secret of life. The first was the structure of DNA. The theory as published by Monod et al. (1963) was concerned chiefly with cooperativity and feedback inhibition of enzymes, such as the inhibition of threonine deaminase, the first enzyme in the pathway of the synthesis of isoleucine, by isoleucine, and its activation by valine. Two years later the theory was formalized by Monod et al. (1965).

Citations

• Genetic regulatory mechanisms in the synthesis of proteins
• Hydrogen exchange and structural dynamics of proteins and nucleic acids

Cited by

• Functional analyses identify the L1 ORF2p Cryptic domain as a hub for intramolecular interfaces required for retrotransposition
• Brain nicotinic receptors: structure and regulation, role in learning and reinforcement
• Combining Small-Molecule Bioconjugation and Hydrogen–Deuterium Exchange Mass Spectrometry (HDX-MS) to Expose Allostery: the Case of Human Cytochrome P450 3A4

Related

• Intermolecular Enzymatic Encoding of Nucleic Acid, Steroid Complexes: A New Theory on the Chemical Origin of Life Based on Evidence of Structural Symmetry
• Mixed Anhydrides at the Intersection Between Peptide and RNA Autocatalytic Sets: Evolution of Biological Coding
• The Adaptation of Complexity in the Evolution of Macromolecules
• A Novel Mathematical Model of Protein Interactions from the Perspective of Electron Delocalization
• A Unified View of Allostery