Cooperative hemoglobins: conserved fold, diverse quaternary assemblies and allosteric mechanisms.
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.
Royer
W E
WE
Dept of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, USA. William.Royer@umassmed.edu
Knapp
J E
JE
Strand
K
K
Heaslet
H A
HA
D000495:Allosteric Site; D000818:Animals; D019281:Dimerization; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
D006454:Hemoglobins; D008024:Ligands