1ms7
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(New page: 200px<br /><applet load="1ms7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ms7, resolution 1.97Å" /> '''X-ray structure of t...)
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Revision as of 19:32, 20 November 2007
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X-ray structure of the GluR2 ligand-binding core (S1S2J) in complex with (S)-Des-Me-AMPA at 1.97 A resolution, Crystallization in the presence of zinc acetate
Overview
X-ray structures of the GluR2 ligand-binding core in complex with, (S)-Des-Me-AMPA and in the presence and absence of zinc ions have been, determined. (S)-Des-Me-AMPA, which is devoid of a substituent in the, 5-position of the isoxazolol ring, only has limited interactions with the, partly hydrophobic pocket of the ligand-binding site, and adopts an, AMPA-like binding mode. The structures, in comparison with other agonist, complex structures, disclose the relative importance of the isoxazolol, ring and of the substituent in the 5-position for the mode of binding. A, relationship appears to exist between the extent of interaction of the, ligand with the hydrophobic pocket and the affinity of the ligand.
About this Structure
1MS7 is a Single protein structure of sequence from Rattus norvegicus with ZN and SHI as ligands. Full crystallographic information is available from OCA.
Reference
GluR2 ligand-binding core complexes: importance of the isoxazolol moiety and 5-substituent for the binding mode of AMPA-type agonists., Kasper C, Lunn ML, Liljefors T, Gouaux E, Egebjerg J, Kastrup JS, FEBS Lett. 2002 Nov 6;531(2):173-8. PMID:12417307
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