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• W2111729275 endingPage "1698" @default.
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• W2111729275 abstract "Allosteric regulation of protein function occurs when the regulatory trigger, such as the binding of a small-molecule effector or inhibitor, takes place some distance from the protein's, or protein complex's, active site. This distance can be a few A, or tens of A. Many proteins are regulated in this way and exhibit a variety of allosteric mechanisms. Here we review how analyses of experimentally determined models of protein 3D structures, using either X-ray crystallography or NMR spectroscopy, have revealed some of the mechanisms involved." @default.
• W2111729275 created "2016-06-24" @default.
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• W2111729275 date "2009-03-18" @default.
• W2111729275 modified "2023-09-30" @default.
• W2111729275 title "The structural basis of allosteric regulation in proteins" @default.
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• W2111729275 doi "https://doi.org/10.1016/j.febslet.2009.03.019" @default.
• W2111729275 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19303011" @default.
• W2111729275 hasPublicationYear "2009" @default.
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