Cooperative hemoglobins: conserved fold, diverse quaternary assemblies and allosteric mechanisms
Graduate School of Biomedical Sciences; Dept of Biochemistry and Molecular Pharmacology
Medical Subject Headings
Allosteric Site; Animals; Dimerization; Hemoglobins; Humans; Ligands; Models, Molecular; Protein Binding; Protein Folding; Protein Structure, Quaternary; Protein Structure, Tertiary
Life Sciences | Medicine and Health Sciences
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.
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Citation: Trends Biochem Sci. 2001 May;26(5):297-304.
Trends in biochemical sciences
Royer, William E.; Knapp, James E.; Strand, Kristen; and Heaslet, Holly A., "Cooperative hemoglobins: conserved fold, diverse quaternary assemblies and allosteric mechanisms" (2001). GSBS Student Publications. 1028.