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Allosteric regulation of an enzyme. In the fields of biochemistry and pharmacology an allosteric regulator (or allosteric modulator) is a substance that binds to a site on an enzyme or receptor distinct from the active site, resulting in a conformational change that alters the protein's activity, either enhancing or inhibiting its function.
An allosteric transition of a protein between R and T states, stabilised by an Agonist, an Inhibitor and a Substrate. In biochemistry, the Monod–Wyman–Changeux model (MWC model, also known as the symmetry model or concerted model) describes allosteric transitions of proteins made up of identical subunits.
In biochemistry, allosteric regulation (or allosteric control) is the regulation of a protein by binding an effector molecule at a site other than the enzyme's active site. The site to which the effector binds is termed the allosteric site .
The site that an allosteric modulator binds to (i.e., an allosteric site) is not the same one to which an endogenous agonist of the receptor would bind (i.e., an orthosteric site). Modulators and agonists can both be called receptor ligands. [2] Allosteric modulators can be 1 of 3 types either: positive, negative or neutral.
The morpheein model of allosteric regulation has similarities to and differences from other models. [1] [6] [11] The concerted model (the Monod, Wyman and Changeux (MWC) model) of allosteric regulation requires all subunits to be in the same conformation or state within an oligomer like the morpheein model.
The sequential model (also known as the KNF model) is a theory that describes cooperativity of protein subunits. [1] It postulates that a protein's conformation changes with each binding of a ligand , thus sequentially changing its affinity for the ligand at neighboring binding sites.
A regulatory domain (sometimes called the core domain, which binds allolactose, an allosteric effector molecule) A linker that connects the DNA-binding domain with the core domain (sometimes called the hinge helix, which is important for allosteric communication [6]) A C-terminal tetramerization region (which joins four monomers in an alpha ...
The allosteric regulators are shown as sphere models. This particular structure of GLUD1 is a combination of two X-ray structures - one with a bound GTP and the second one with a bound ADP (1NQT,8AR8). Although not real, this structure shows the relative position of the allosteric effectors when bound to GLUD1. NADPH and Glu are shown as well.