3tkd
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
[[Image:3tkd.png|left|200px]] | [[Image:3tkd.png|left|200px]] | ||
| - | <!-- | ||
| - | The line below this paragraph, containing "STRUCTURE_3tkd", creates the "Structure Box" on the page. | ||
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| - | or leave the SCENE parameter empty for the default display. | ||
| - | --> | ||
{{STRUCTURE_3tkd| PDB=3tkd | SCENE= }} | {{STRUCTURE_3tkd| PDB=3tkd | SCENE= }} | ||
===Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and cyclothiazide at 1.45 A resolution=== | ===Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and cyclothiazide at 1.45 A resolution=== | ||
| - | |||
| - | <!-- | ||
| - | The line below this paragraph, {{ABSTRACT_PUBMED_21895609}}, adds the Publication Abstract to the page | ||
| - | (as it appears on PubMed at http://www.pubmed.gov), where 21895609 is the PubMed ID number. | ||
| - | --> | ||
{{ABSTRACT_PUBMED_21895609}} | {{ABSTRACT_PUBMED_21895609}} | ||
| Line 22: | Line 11: | ||
==See Also== | ==See Also== | ||
| - | *[[Ionotropic Glutamate Receptors]] | + | *[[Ionotropic Glutamate Receptors|Ionotropic Glutamate Receptors]] |
==Reference== | ==Reference== | ||
Revision as of 11:04, 25 July 2012
Contents |
Crystal structure of the GluA2 ligand-binding domain (S1S2J-L483Y-N754S) in complex with glutamate and cyclothiazide at 1.45 A resolution
Template:ABSTRACT PUBMED 21895609
About this Structure
3tkd is a 2 chain structure of Ionotropic Glutamate Receptors with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
See Also
Reference
- Krintel C, Frydenvang K, Olsen L, Kristensen MT, de Barrios O, Naur P, Francotte P, Pirotte B, Gajhede M, Kastrup JS. Thermodynamics and structural analysis of positive allosteric modulation of the ionotropic glutamate receptor GluA2. Biochem J. 2011 Sep 7. PMID:21895609 doi:10.1042/BJ20111221
- Sun Y, Olson R, Horning M, Armstrong N, Mayer M, Gouaux E. Mechanism of glutamate receptor desensitization. Nature. 2002 May 16;417(6886):245-53. PMID:12015593 doi:10.1038/417245a
