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1nnp
From Proteopedia
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[[Image:1nnp.gif|left|200px]] | [[Image:1nnp.gif|left|200px]] | ||
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'''X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-ATPA at 1.9 A resolution. Crystallization without zinc ions.''' | '''X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-ATPA at 1.9 A resolution. Crystallization without zinc ions.''' | ||
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[[Category: Lunn, M L.]] | [[Category: Lunn, M L.]] | ||
[[Category: Stensbol, T B.]] | [[Category: Stensbol, T B.]] | ||
| - | [[Category: | + | [[Category: Agonist complex.]] |
| - | [[Category: | + | [[Category: Ionotropic glutamate receptor glur2]] |
| - | [[Category: | + | [[Category: Ligand-binding core]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:45:19 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:45, 2 May 2008
X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-ATPA at 1.9 A resolution. Crystallization without zinc ions.
Overview
Two X-ray structures of the GluR2 ligand-binding core in complex with (S)-2-amino-3-(5-tert-butyl-3-hydroxy-4-isoxazolyl)propionic acid ((S)-ATPA) have been determined with and without Zn(2+) ions. (S)-ATPA induces a domain closure of ca. 21 degrees compared to the apo form. The tert-butyl moiety of (S)-ATPA is buried in a partially hydrophobic pocket and forces the ligand into the glutamate-like binding mode. The structures provide new insight into the molecular basis of agonist selectivity between AMPA and kainate receptors.
About this Structure
1NNP is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity., Lunn ML, Hogner A, Stensbol TB, Gouaux E, Egebjerg J, Kastrup JS, J Med Chem. 2003 Feb 27;46(5):872-5. PMID:12593667 Page seeded by OCA on Sat May 3 02:45:19 2008
