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Titolo:
Evidence for a direct interaction between the penultimate aspartic acid ofcholecystokinin and histidine 207, located in the second extracellular loop of the cholecystokinin B receptor
Autore:
Silvente-Poirot, S; Escrieut, C; Gales, C; Fehrentz, JA; Escherich, A; Wank, SA; Martinez, J; Moroder, L; Maigret, B; Bouisson, M; Vaysse, N; Fourmy, D;
Indirizzi:
CHU Rangueil, INSERM U151, Inst Louis Bugnart, F-31403 Toulouse, France CHU Rangueil Toulouse France F-31403 s Bugnart, F-31403 Toulouse, France Univ Nancy, Chim Theor Lab, F-54506 Vandoeuvre Nancy, France Univ Nancy Vandoeuvre Nancy France F-54506 4506 Vandoeuvre Nancy, France NIDDK, Digest Dis Branch, NIH, Bethesda, MD 20892 USA NIDDK Bethesda MD USA 20892 igest Dis Branch, NIH, Bethesda, MD 20892 USA Max Planck Inst Biochem, D-82143 Martinsried, Germany Max Planck Inst Biochem Martinsried Germany D-82143 Martinsried, Germany
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 33, volume: 274, anno: 1999,
pagine: 23191 - 23197
SICI:
0021-9258(19990813)274:33<23191:EFADIB>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
BETA-ADRENERGIC-RECEPTOR; FUNCTIONAL EXPRESSION; ANGIOTENSIN-II; MUTANT CYCLES; A RECEPTOR; ANTAGONISTS; BINDING; SELECTIVITY; ACTIVATION; RESIDUE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Silvente-Poirot, S CHU Rangueil, INSERM U151, Inst Louis Bugnart, Bat L3, F-31403 Toulouse, France CHU Rangueil Bat L3 Toulouse France F-31403 se, France
Citazione:
S. Silvente-Poirot et al., "Evidence for a direct interaction between the penultimate aspartic acid ofcholecystokinin and histidine 207, located in the second extracellular loop of the cholecystokinin B receptor", J BIOL CHEM, 274(33), 1999, pp. 23191-23197

Abstract

Recently, we reported that the mutation of His(207) to Phe located in the second extracellular loop of the cholecystokinin B receptor strongly affected cholecystokinin (CCK) binding (Silvente-Poirot, S., Escrieut, C., and Wank, S. A. (1998) Mol. Pharmacol. 54, 364-371), To characterize the functional group in CCK that interacts with His(207), we first substituted His(207)to Ala. This mutation decreased the affinity and the potency of CCK to produce total inositol phosphates 302-fold and 456-fold without affecting the expression of the mutant receptor. The screening of L-alanine-modified CCK peptides to bind and activate the wild type and mutant receptors allowed the identification of the interaction of the C-terminal Asp(8) of CCK with His(207). The H207A-CCKBR mutant, unlike the wild type receptor, was insensitive to substitution of Asp(8) of CCK to other amino acid residues. This interaction was further confirmed by mutating His(207) to Asp, The affinity ofCCK for the H207D-CCKBR mutant was 100-fold lower than for the H207ACCKBR mutant, consistent with an electrostatic repulsion between the negative charges of the two interacting aspartic acids. Peptides with neutral amino acids in position eight of CCK reversed this effect and displayed a gain of affinity for the H207D mutant compared with CCK. To date, this is the first report concerning the identification of a direct contact point between the CCKB receptor and CCK.

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Documento generato il 01/10/20 alle ore 16:18:22