01452nam a2200217 a 450000100080000000500110000800800410001910000160006024501650007626001600024130000190040152006190042065000190103965000310105865300200108965300420110965300160115165300350116770000160120270000160121819141032020-01-13       2011    bl uuuu     u00u1 u    #d1 aNESHICH, I.  aStructural characterization of MK-801 binding site through spatial and physical-chemical properties on NMDAr-mimicking AMPA-Glur mutants.h[electronic resource]  aIn: ANNUAL MEETING OF THE SBBq, 40., 2011, Foz do Iguaçu. [Proceedings...]. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biologyc2011  aNão paginado.  aComputational Biology approaches including modeling, dynamics and docking of these compounds to the channel pore region were used. Interestingly, we found that MK-801 had better docking score values against AMPA GluR mutants than to AMPA Wild Type receptor, which is in agreement with the inhibition potency (Ki values) described in the literature. We also suggest a mechanism of binding of MK-801 to GluR and we provided a structural explanation for the MK-801 greater potency of inhibition on triple mutant compared to the double mutant. These results can provide insights on NMDA receptors inhibition by MK-801.  aBioinformatics  aPhysicochemical properties  aBioinformática  aCaracterização estrutural de MK-801  aDizocilpine  aPropriedades físico-químicas1 aHAYASHI, M.1 aNESHICH, G.