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Titolo:
Primary structures of PYY, [Pro(34)]PYY, and PYY-(3-36) confer different conformations and receptor selectivity
Autore:
Keire, DA; Mannon, P; Kobayashi, M; Walsh, JH; Solomon, TE; Reeve, JR;
Indirizzi:
Greater Los Angeles Vet Affairs Healthcare Syst, CURE Digest Dis Res Ctr, Los Angeles, CA 90073 USA Greater Los Angeles Vet Affairs Healthcare Syst Los Angeles CA USA 90073 City Hope Natl Med Ctr, Beckman Res Inst, Duarte, CA 91010 USA City Hope Natl Med Ctr Duarte CA USA 91010 Res Inst, Duarte, CA 91010 USA Vet Affairs Med Ctr, Durham, NC 27705 USA Vet Affairs Med Ctr Durham NC USA 27705 irs Med Ctr, Durham, NC 27705 USA Duke Univ, Med Ctr, Durham, NC 27705 USA Duke Univ Durham NC USA 27705Duke Univ, Med Ctr, Durham, NC 27705 USA Univ Calif Los Angeles, Sch Med, Div Digest Dis, Los Angeles, CA 90095 USAUniv Calif Los Angeles Los Angeles CA USA 90095 Los Angeles, CA 90095 USA
Titolo Testata:
AMERICAN JOURNAL OF PHYSIOLOGY-GASTROINTESTINAL AND LIVER PHYSIOLOGY
fascicolo: 1, volume: 279, anno: 2000,
pagine: G126 - G131
SICI:
0193-1857(200007)279:1<G126:PSOP[A>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMPHIPHILIC SECONDARY STRUCTURES; HUMAN NEUROPEPTIDE-Y; PEPTIDE-YY; PANCREATIC-POLYPEPTIDE; AQUEOUS-SOLUTION; Y-2 RECEPTORS; ANALOGS; BINDING; DYNAMICS; CELLS;
Keywords:
peptide YY; Y-1 receptor; Y-2 receptor; circular dichroism; nuclear magnetic resonance; three-dimensional structure;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Reeve, JR Greater Los Angeles Vet Affairs Healthcare Syst, CURE Digest DisRes Ctr, Rm 115,Bld 115, Los Angeles, CA 90073 USA Greater Los Angeles VetAffairs Healthcare Syst Rm 115,Bld 115 Los Angeles CA USA 90073
Citazione:
D.A. Keire et al., "Primary structures of PYY, [Pro(34)]PYY, and PYY-(3-36) confer different conformations and receptor selectivity", AM J P-GAST, 279(1), 2000, pp. G126-G131

Abstract

We synthesized PYY-(1-36) (nonselective between Y-1 and Y-2 receptor subtype agonists), [Pro(34)]-PYY (selective for Y-1), and PYY-(3-36) (selective for Y-2) to determine whether solution conformation plays a role in receptor subtype selectivity. The three peptides exhibited the expected specificities in displacing labeled PYY-(1-36) from cells transfected with Y-1 receptors (dissociation constants = 0.42, 0.21, and 1,050 nM, respectively) and from cells transfected with Y2 receptors (dissociation constants = 0.03, 710, and 0.11 nM, respectively) for PYY-(1-36), [Pro(34)]PYY, and PYY-(3-36). Sedimentation equilibrium analyses revealed that the three PYY analogs were80-90% monomer at the concentrations used for the subsequent circular dichroism (CD) and H-1-nuclear magnetic resonance (NMR) studies. CD analysis measured helicities for PYY-(1-36), [Pro(34)]PYY, and PYY-(3-36) of 42%, 31%,and 24%, suggesting distinct differences in secondary structure. The backbone H-1-NMR resonances of the three peptides further substantiated marked conformational differences. These patterns support the hypothesis that Y-1 and Y-2 receptor subtype binding affinities depend on the secondary and tertiary solution state structures of PYY and its analogs.

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Documento generato il 27/11/20 alle ore 00:25:34