allosterism


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al·lo·ster·ism

, allostery (ă-los'ter-izm, -los'ter-ē),
The influencing of an enzyme activity, or the binding of a ligand to a protein, by a change in the conformation of the protein, brought about by the binding of a substrate or other effector at a site (allosteric site) other than the active site of the protein. Compare: cooperativity, hysteresis.

allostery

A phenomenon in which a ligand binds to a specific receptor site on a protein, changing its shape, and altering the affinity for a ligand at a second site (e.g., either a receptor or a binding site); the ability of an effector molecule (ligand) to change the conformation and activity of a protein.

In allostery, the catalytic function of an enzyme may be modified by interaction with small molecules, not only at the active site but also at a spatially distinct (allosteric) site of different specificity. Allostery refers to an interaction of two or more functional sites on a protein, or two or more proteins, resulting in altered affinity of ligand binding; it depends on dynamic interaction with a substrate or other molecule—e.g., heme-heme interaction.

al·lo·ster·ism

, allostery (al'ō-ster'izm, al'ō-ster'ē)
The influencing of an enzyme activity, or the binding of a ligand to a protein, by a change in the conformation of the protein, brought about by the binding of a substrate or other effector at a site (allosteric site) other than the active site of the protein.
Compare: hysteresis
References in periodicals archive ?
Federico, 2017, "Models, Theory Structure and Mechanisms in Biochemistry: The Case of Allosterism", Studies in History and Philosophy of Science Part C: Studies in History and Philosophy of Biological and Biomedical Sciences, no.
These findings were published online in the peer-reviewed journal 'Molecular Pharmacology (Lateral Allosterism in the Glucagon Receptor Family: GLP-1 Induces GPCR Heteromer Formation [Schelshorn et al', Molecular Pharmacology, Published online, doi: 10.1124/mol.111.074757]).
Structure, function and interfacial allosterism in phospholipase A2: insight from the anion-assisted dimer.