Structural asymmetry and half-site reactivity in the T to R allosteric transition of the insulin hexamer.

doi:10.1021/bi00248a015

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Article

Structural asymmetry and half-site reactivity in the T to R allosteric transition of the insulin hexamer.

Biochemistry - 8 Nov 1994

Brzović P S, Choi W E, Borchardt D, Kaarsholm N C, Dunn M F

Abstract excerpt

The zinc-insulin hexamer, the storage form of insulin in the pancreas, is an allosteric protein capable of undergoing transitions between three distinct conformational states, designated T6, T3R3, and R6, on the basis of their ligand binding properties, allosteric behavior, and pseudo point symme...

Topics

Allosteric Regulation
Anions
Binding Sites
Humans
Insulin
Ligands
Magnetic Resonance Spectroscopy
Models, Molecular
Mutation
Phenols
Polymers
Protein Conformation
Protein Structure, Secondary
Recombinant Proteins
Zinc

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