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Titolo:
Mutant cycle analysis of the active and desensitized states of an AMPA receptor induced by willardiines
Autore:
Kizelsztein, P; Eisenstein, M; Strutz, N; Hollmann, M; Teichberg, VI;
Indirizzi:
Weizmann Inst Sci, Dept Neurobiol, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 biol, IL-76100 Rehovot, Israel Weizmann Inst Sci, Dept Chem Serv, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 Serv, IL-76100 Rehovot, Israel Lab Glutamate Receptor Res, Gottingen, Germany Lab Glutamate Receptor ResGottingen Germany or Res, Gottingen, Germany Max Planck Inst Expt Med, D-3400 Gottingen, Germany Max Planck Inst Expt Med Gottingen Germany D-3400 400 Gottingen, Germany
Titolo Testata:
BIOCHEMISTRY
fascicolo: 42, volume: 39, anno: 2000,
pagine: 12819 - 12827
SICI:
0006-2960(20001024)39:42<12819:MCAOTA>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
SYNAPTIC TRANSMISSION; KAINATE RECEPTORS; SITE; CYCLOTHIAZIDE; ACTIVATION; CHANNEL; MODULATION; COMPLEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Teichberg, VI Weizmann Inst Sci, Dept Neurobiol, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 Rehovot, Israel
Citazione:
P. Kizelsztein et al., "Mutant cycle analysis of the active and desensitized states of an AMPA receptor induced by willardiines", BIOCHEM, 39(42), 2000, pp. 12819-12827

Abstract

The halogenated willardiines are agonists at the alpha -amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) subtype of glutamate receptors. Although they differ only by the nature of the halogen substituent, they display marked differences in their efficacy to activate the receptor channel opening and in causing desensitization. We have studied the origin of the different agonist properties of the willardiines and in particular the nature of the structural element within the receptor binding domain that is able To distinguish between willardiines at a subatomic resolution of 0.6 Angstrom (the difference in radius between F and Br) and allow (S)-5-fluorowillardiine to cause receptor desensitization much more than (S)-5-bromowillardiine. For this purpose, we analyzed, with the thermodynamic mutant cycle method, the active and desensitized states induced by the willardiines in the GluR1 subtype of AMPA receptors and GLuR1 mutants in which residues E398, Y446, L646, and S650, within the agonist binding domain, were mutated. The results were used to generate a 3D model of the willardiine docking mode. We suggest that the active and desensitized states of the AMPA-R correspond, respectively, to the open-lobe and closed-lobe conformations of the agonist binding domain.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 20:55:20