GSBS Student Publications

Title

Cooperative hemoglobins: conserved fold, diverse quaternary assemblies and allosteric mechanisms

UMMS Affiliation

Graduate School of Biomedical Sciences; Dept of Biochemistry and Molecular Pharmacology

Date

5-10-2001

Document Type

Article

Medical Subject Headings

Allosteric Site; Animals; Dimerization; Hemoglobins; Humans; Ligands; Models, Molecular; Protein Binding; Protein Folding; Protein Structure, Quaternary; Protein Structure, Tertiary

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

Assembly of hemoglobin subunits into cooperative complexes produces a remarkable variety of architectures, ranging in oligomeric state from dimers to complexes containing 144 hemoglobin subunits. Diverse stereochemical mechanisms for modulating ligand affinity through intersubunit interactions have been revealed from studies of three distinct hemoglobin assemblages. This mechanistic diversity, which occurs between assemblies of subunits that have the same fold, provides insight into the range of regulatory strategies that are available to protein molecules.

Rights and Permissions

Citation: Trends Biochem Sci. 2001 May;26(5):297-304.

Related Resources

Link to Article in PubMed

Journal Title

Trends in biochemical sciences

PubMed ID

11343922