Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: Implications for receptor subunit selectivity

Marie Louise Lunn, Anders Hogner, Tine B. Stensbøl, Eric Gouaux, Jan Egebjerg, Jette S. Kastrup

Research output: Contribution to journalArticle

47 Scopus citations

Abstract

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 Zn2+ ions. (S)-ATPA induces a domain closure of ca. 21° 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.

Original languageEnglish (US)
Pages (from-to)872-875
Number of pages4
JournalJournal of Medicinal Chemistry
Volume46
Issue number5
DOIs
StatePublished - Feb 27 2003
Externally publishedYes

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ASJC Scopus subject areas

  • Organic Chemistry

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