Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 171685
Author(s) Stern-Bach, Y; Bettler, B; Hartley, M; Sheppard, P O; O'Hara, P J; Heinemann, S F
Author(s) at UniBasel Bettler, Bernhard
Year 1994
Title Agonist selectivity of glutamate receptors is specified by two domains structurally related to bacterial amino acid-binding proteins
Journal Neuron
Volume 13
Number 6
Pages / Article-Number 1345-57
Abstract

By exchanging portions of the AMPA receptor subunit GluR3 and the kainate receptor subunit GluR6, we have identified two discontinuous segments of approximately 150 amino acid residues each that control the agonist pharmacology of these glutamate receptors. The first segment (S1) is adjacent and N-terminal to the putative transmembrane domain 1 (TM1), whereas the second segment (S2) is located between the putative TM3 and TM4. Only the simultaneous exchange of S1 and S2 converts the pharmacological profile of the recipient to that of the donor subunit. The two segments identified in this study share sequence similarities with the ligand-binding site of several bacterial periplasmic amino acid-binding proteins. Based on the X-ray structure of these proteins, we propose a model for the glutamate-binding site of ionotropic glutamate receptors.

Publisher Cell Press
ISSN/ISBN 0896-6273
edoc-URL http://edoc.unibas.ch/dok/A5262296
Full Text on edoc No
Digital Object Identifier DOI 10.1016/0896-6273(94)90420-0
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/7527641
ISI-Number WOS:A1994PZ68900009
Document type (ISI) Journal Article
 
   

MCSS v5.8 PRO. 0.493 sec, queries - 0.000 sec ©Universität Basel  |  Impressum   |    
07/08/2020