3o28 | pdb_00003o28
From Proteopedia
Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator
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Structural highlights
Evolutionary ConservationCheck, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStarting from an HTS derived hit 1, application of biostructural data facilitated rapid optimization to lead 22, a novel AMPA receptor modulator. This is the first demonstration of how structure based drug design can be exploited in an optimization program for a glutamate receptor. A novel series of positive modulators of the AMPA receptor: Discovery and structure based hit-to-lead studies.,Jamieson C, Basten S, Campbell RA, Cumming IA, Gillen KJ, Gillespie J, Kazemier B, Kiczun M, Lamont Y, Lyons AJ, Maclean JK, Moir EM, Morrow JA, Papakosta M, Rankovic Z, Smith L Bioorg Med Chem Lett. 2010 Oct 1;20(19):5753-6. Epub 2010 Aug 13. PMID:20805031[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 13:04, 9 December 2014.