Alignment of weakly interacting molecules to protein surfaces using simulations of chemical shift perturbations.
Structural studies of protein-ligand complexes are often limited by low solubility, poor affinity, and interfacial motion and, in NMR structures, by the lack of intermolecular NOEs. In the absence of other structural restraints, we use a procedure that compares simulated chemical shift perturbations to observed perturbations to better define the binding orientation of ligands with respect to protein surfaces.
McCoy
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MA
Schering-Plough Research Institute, Kenilworth, NJ 07033, USA. mark.mccoy@spcorp.com
Wyss
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D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000737:chemistry / Q000378:metabolism; D002147:Calmodulin / Q000737:chemistry / Q000378:metabolism; D003198:Computer Simulation; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D013449:Sulfonamides / Q000737:chemistry / Q000378:metabolism
D002147:Calmodulin; D004791:Enzyme Inhibitors; D008024:Ligands; D011506:Proteins; D013449:Sulfonamides; C017967:W 7; D002118:Calcium