3o28: Difference between revisions
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[[Image:3o28.png|left|200px]] | [[Image:3o28.png|left|200px]] | ||
{{STRUCTURE_3o28| PDB=3o28 | SCENE= }} | {{STRUCTURE_3o28| PDB=3o28 | SCENE= }} | ||
===Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator=== | ===Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator=== | ||
{{ABSTRACT_PUBMED_20805031}} | {{ABSTRACT_PUBMED_20805031}} | ||
==About this Structure== | ==About this Structure== | ||
[[3o28]] is a 1 chain structure of [[Ionotropic Glutamate Receptors]] with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O28 OCA]. | |||
==See Also== | |||
*[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:020805031</ref><references group="xtra"/> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Basten, S.]] | [[Category: Basten, S.]] | ||
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[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 04:23, 27 July 2012
Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator
Template:ABSTRACT PUBMED 20805031
About this Structure
3o28 is a 1 chain structure of Ionotropic Glutamate Receptors with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
See Also
Reference
- 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. A novel series of positive modulators of the AMPA receptor: Discovery and structure based hit-to-lead studies. Bioorg Med Chem Lett. 2010 Oct 1;20(19):5753-6. Epub 2010 Aug 13. PMID:20805031 doi:10.1016/j.bmcl.2010.07.138
