allostery


Also found in: Dictionary, Encyclopedia, Wikipedia.
Related to allostery: angiostenosis, analgia, arthrosteitis

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

/al·lo·ste·ry/ (al´o-ster″e) the condition in which binding of a substrate, product, or other effector to a subunit of a multi-subunit enzyme at a site (allosteric site) other than the functional site alters its conformation and functional properties.

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
Mentioned in ?
References in periodicals archive ?
We are looking at several problems, such as drug discovery, protein analysis, allostery and virus particles," he says.
Certainly, this model of allostery presumes an 'extra-soft' and highly dynamic protein structure, and complicates the presentation of the ligand recognition mechanism in terms used by conventional structural biology, counting the presence or absence of distinct interactions between ligand and protein molecules.
Importantly, an action in one domain could affect other, distally located sites, an event termed allostery (Kern and Zuiderweg 2004).
This property is allostery, and a protein is allosteric if it can increase or decrease its ability to participate in a reaction.