Examples of allosteric in the following topics:
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- In noncompetitive allosteric inhibition, inhibitor molecules bind to an enzyme at the allosteric site.
- However, allosteric inhibitors are not the only molecules that bind to allosteric sites.
- Allosteric activators can increase reaction rates.
- However, while ATP is an inhibitor, ADP is an allosteric activator.
- Allosteric inhibitors modify the active site of the enzyme so that substrate binding is reduced or prevented.
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- A number of enzymes involved in each of the pathways (in particular, the enzyme catalyzing the first committed reaction of the pathway) are controlled by attachment of a molecule to an allosteric (non-active) site on the protein.
- These regulators, known as allosteric effectors, may increase or decrease enzyme activity, depending on the prevailing conditions, altering the steric structure of the enzyme, usually affecting the configuration of the active site.
- The attachment of a molecule to the allosteric site serves to send a signal to the enzyme, providing feedback.
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- Antagonists mediate their effects by binding to the active site or to allosteric sites on receptors, or they may interact at unique binding sites not normally involved in the biological regulation of the receptor's activity.
- The term "non-competitive antagonism" (sometimes called non-surmountable antagonists) can be used to describe two distinct phenomena: one in which the antagonist binds to the active site of the receptor, and one in which the antagonist binds to an allosteric site of the receptor.
- The second form of "non-competitive antagonists" act at an allosteric site.
- Uncompetitive antagonists differ from non-competitive antagonists in that they require receptor activation by an agonist before they can bind to a separate allosteric binding site.
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- It is allosterically stimulated by NADP+.
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- Two cAMP molecules bind dimeric CAP with negative cooperativity and function as allosteric effectors by increasing the protein's affinity for DNA.
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- Phage display technology is advantageous in many applications including selection of inhibitors for the active and allosteric sites of enzymes, receptor agonists and antagonists, and G-protein binding modulatory peptides.
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- Ionotropic receptors are a group of transmembrane ion channels that open or close in response to the binding of a chemical messenger (ligand) such as a neurotransmitter.The binding site of endogenous ligands on LGICs protein complexes are normally located on a different portion of the protein (an allosteric binding site) than the location of the ion conduction pore.The ion channel is regulated by a ligand and is usually very selective to one or more ions such as Na+, K+, Ca2+, or Cl-.
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- B) ATP binds to component II, which receives electrons from an electron donor (ferredoxin or flavodoxin); binding of ATP induces an allosteric conformational change which allows association of the two proteins.
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- Pyruvate kinase is also regulated by ATP (a negative allosteric effect).
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- However, because of allosteric effects on the hemoglobin molecule, the binding of carbon dioxide decreases the amount of oxygen bound for a given partial pressure of oxygen.