3O29

Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator

Summary for 3O29

• Entry DOI: 10.2210/pdb3o29/pdb
• Related: 3O28 3O2A 3O6G 3O6H 3O6I 3PMV 3PMW 3PMX
• Descriptor: Glutamate receptor 2, GLUTAMIC ACID, SULFATE ION, ... (6 entities in total)
• Functional Keywords: transport protein, membrane protein, fusion protein, chimera protein
• Biological source: Rattus norvegicus (rat); More
• Cellular location: Cell membrane; Multi-pass membrane protein: P19491
• Total number of polymer chains: 1
• Total formula weight: 30382.88

Authors

Maclean, J.K.F.,Basten, S.,Campbell, R.A.,Cumming, I.A.,Gillen, K.J.,Gillespie, J.,Jamieson, C.,Kazemier, B.,Kiczun, M.,Lamont, Y.,Lyons, A.J.,Moir, E.M.,Morrow, J.A.,Papakosta, M.,Rankovic, Z.,Smith, L. (deposition date: 2010-07-22, release date: 2010-09-15, Last modification date: 2024-11-06)

Primary citation

Jamieson, C.,Basten, S.,Campbell, R.A.,Cumming, I.A.,Gillen, K.J.,Gillespie, J.,Kazemier, B.,Kiczun, M.,Lamont, Y.,Lyons, A.J.,Maclean, J.K.,Moir, E.M.,Morrow, J.A.,Papakosta, M.,Rankovic, Z.,Smith, L.
A novel series of positive modulators of the AMPA receptor: discovery and structure based hit-to-lead studies.
Bioorg.Med.Chem.Lett., 20:5753-5756, 2010

PubMed Abstract: Starting 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.

PubMed: 20805031
DOI: 10.1016/j.bmcl.2010.07.138

Experimental method

X-RAY DIFFRACTION (2.02 Å)