allostery


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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
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References in periodicals archive ?
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.
Interestingly, this inversion of allostery was observed experimentally for peptide LRAASLG, as the affinity of protein kinase A for this substrate was quite significantly below the critical limit.
This means that at least this part of the substrate specificity of protein kinase A that is based on the recognition of the primary structure of phosphorylatable peptides is amplified by allostery.
This relationship had a significant negative intercept at the y-axis, revealing inversion of the allosteric effect: the positive allostery for good substrates changed to negative allostery for bad substrates in this model reaction of regulatory phosphorylation.
Protein dynamics and long-range allostery in cell signaling
They discuss structural characterization of EPAC by x-ray crystallography; sensory neuron cAMP signaling in chronic pain; monitoring real-time cyclic nucleotide dynamics in subcellular microdomains; identifying complexes of adenylyl with A-kinase anchoring proteins; assessing cyclic nucleotide binding domain allostery and dynamics by nuclear magnetic resonance spectroscopy; a protocol for expression and purification of cyclic nucleotide-free protein in E.