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Titolo:
MUTATIONAL ANALYSIS OF THE PUTATIVE DEVAZEPIDE BINDING-SITE OF THE CCKA RECEPTOR
Autore:
SMEETS RLL; IJZERMAN AP; HERMSEN HPH; OPHORST OJAE; VRIES SEV; DEPONT JJHHM; WILLEMS PHGM;
Indirizzi:
UNIV NIJMEGEN,DEPT BIOCHEM,POB 9101 NL-6500 HB NIJMEGEN NETHERLANDS UNIV NIJMEGEN,DEPT BIOCHEM NL-6500 HB NIJMEGEN NETHERLANDS LEIDEN AMSTERDAM CTR DRUG RES,DIV MED CHEM LEIDEN NETHERLANDS HOGESCH GELDERLAND NIJMEGEN NETHERLANDS
Titolo Testata:
European journal of pharmacology
fascicolo: 1, volume: 325, anno: 1997,
pagine: 93 - 99
SICI:
0014-2999(1997)325:1<93:MAOTPD>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
PANCREATIC ACINAR-CELLS; PROTEIN-KINASE-C; CHOLECYSTOKININ RECEPTOR; AFFINITY-STATE; ANTAGONISTS;
Keywords:
CHO (CHINESE HAMSTER OVARY) CELL; CHOLECYSTOKININ; CCKA RECEPTOR; DEVAZEPIDE; L-364,718; CA2+ MOBILIZATION; CELL RECRUITMENT; RECEPTOR MODELING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
17
Recensione:
Indirizzi per estratti:
Citazione:
R.L.L. Smeets et al., "MUTATIONAL ANALYSIS OF THE PUTATIVE DEVAZEPIDE BINDING-SITE OF THE CCKA RECEPTOR", European journal of pharmacology, 325(1), 1997, pp. 93-99

Abstract

Recently a molecular model was proposed for the binding site of the antagonist 3S(-)-N-(2,3-dihydro-1-methyl-2-oxo-5-phenyl-1H-1 ,4-benzodiazepine-3-yl)-1H-indole-2-carboxamide (devazepide) on the cholecystokinin-A (CCKA) receptor (Van der Bent et al., 1994. Drug Design Discov. 12, 129-148). Fifteen amino acids were identified, including hydrophilic ones such as Ser(139), Asn(349) and Ser(379), that might interact with the carboxamide moiety in devazepide. To provide mutational evidence for this model, wild-type and mutant receptors (S139A, N349A and S379A) were transiently expressed and compared with respect to the ability of devazepide to inhibit binding of radiolabelled cholecystokinin-(26-33)-peptide amide (CCK-8) and CCK-8-evoked Ca2+ mobilization. The data presented suggest the involvement of the three residues in antagonist binding, although to a different extent. However, it does not seemlikely that hydrogen bonds are the driving force in view of the relatively minor changes in receptor affinity and activity. (C) 1997 Elsevier Science B.V.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 16:18:28