The structural basis of allosteric regulation in proteins |
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| Authors: | Roman A. Laskowski Fabian Gerick |
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| Affiliation: | European Bioinformatics Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SD, United Kingdom |
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| 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 Å, or tens of Å. 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. |
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| Keywords: | BoNT/A, botulinum neurotoxin type A CAK, CDK-activating kinase CDK, cyclin-dependent kinase DAHP, 3-deoxy- smallcaps" >d-arbino-heptulosonate-7-phosphate DAHPS, DAHP synthase DBD, DNA-binding domain DHDPS, dihydrodipicolinate synthase DHFR, dihydrofolate reductase E4P, smallcaps" >d-erythrose-4-phosphate FlAsH, fluorescin arsenical hairpin binder hPTP1E, human tyrosine phosphatase 1E KNF, Koshland, Nemethy and Filmer model MWC, Monod, Wyman and Changeux model NBD, nucleotide binding domain PDB, Protein Data Bank PEP, phosphoenolpyruvate PGDH, phosphoglycerate dehydrogenase PTS, phosphotransferase system RBD, regulatory binding domain SBD, substrate binding domain |
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