allosteric transition

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allosteric transition

The reversible modification of a protein’s conformation and function by an effector molecule that binds at a site other than the active site (e.g., through non-competitive receptor inhibition).
References in periodicals archive ?
According to the canonical model, IFN[gamma] cross-links the IFNGR1 subunit, resulting in allosteric changes to the receptor cytoplasmic domain [12].
It was observed that when cells were treated with IFN[gamma] JAK2 binding shifted from receptor subunit IFNGR2 to IFNGR1, presumably as a result of the allosteric changes referred to above [2, 12].
Allosteric changes can be induced by binding the protein to another protein called a ligand, while the allosteric protein that changes shape is often a receptor.