3o6g | pdb_00003o6g
From Proteopedia
Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator
| ||||||||||||
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 lead compound 1, we demonstrate how X-ray structural data can be used to understand SAR and expediently optimize bioavailability in a novel series of AMPA receptor modulators, furnishing 5 with improved bioavailability and robust in vivo activity. A novel series of positive modulators of the AMPA receptor: Structure-based lead optimization.,Jamieson C, Campbell RA, Cumming IA, Gillen KJ, Gillespie J, Kazemier B, Kiczun M, Lamont Y, Lyons AJ, Maclean JK, Martin F, Moir EM, Morrow JA, Pantling J, Rankovic Z, Smith L Bioorg Med Chem Lett. 2010 Aug 15. PMID:20817521[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||||||||
This page was last modified 13:13, 9 December 2014.