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Low-mode docking search in iGluR homology models implicates three residues in the control of ligand selectivity
Journal article   Peer reviewed

Low-mode docking search in iGluR homology models implicates three residues in the control of ligand selectivity

Jonierr Rodriguez, Luis Carcache and Kathleen S Rein
Journal of molecular recognition, Vol.18(2), pp.183-189
03-2005
DOI: https://doi.org/10.1002/jmr.713
PMID: 15476293

Abstract

Amino Acid Sequence Animals Binding Sites DNA Mutational Analysis Excitatory Amino Acid Agonists - pharmacology Kainic Acid - pharmacology Ligands Models, Molecular Molecular Conformation Molecular Sequence Data Protein Binding Rats Receptors, AMPA - chemistry Receptors, AMPA - drug effects Receptors, AMPA - metabolism Receptors, Kainic Acid - chemistry Receptors, Kainic Acid - drug effects Receptors, Kainic Acid - metabolism Sequence Homology, Amino Acid Structure-Activity Relationship
Homology models of the ionotropic rat kainate receptor iGluR6, based on the ligand binding domains of iGluR2, were constructed. A systematic analysis by low-mode docking searches of kainic acid in homology models of the native iGluR6 receptor, chimeric (iGluR2 and iGluR6) receptors and mutant receptors have identified three residues which influence the conformation of kainic acid in the binding core and hence the affinity for kainic acid. These residues are Leu650, Thr649 and Leu704, all located in domain 2. Leu650 has previously been implicated in the control of selectivity of iGluR2. However, this is the first report that suggests that Thr649 and Leu704 play a role in receptor selectivity.

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