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Titolo:
Solution structure of monomeric peptide YY supports the functional significance of the PP-fold
Autore:
Keire, DA; Kobayashi, M; Solomon, TE; Reeve, JR;
Indirizzi:
Univ Calif Los Angeles, CURE, Digest Dis Res Ctr, Greater Los Angles Vet Hlth Care Syst, Los Angeles, CA 90073 USA Univ Calif Los Angeles Los Angeles CA USA 90073 Los Angeles, CA 90073 USA Univ Calif Los Angeles, Sch Med, Div Digest Dis, Los Angeles, CA 90023 USAUniv Calif Los Angeles Los Angeles CA USA 90023 Los Angeles, CA 90023 USA City Hope Natl Med Ctr, Beckman Res Inst, Div Immunol, Duarte, CA 91010 USA City Hope Natl Med Ctr Duarte CA USA 91010 Immunol, Duarte, CA 91010 USA
Titolo Testata:
BIOCHEMISTRY
fascicolo: 32, volume: 39, anno: 2000,
pagine: 9935 - 9942
SICI:
0006-2960(20000815)39:32<9935:SSOMPY>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; HUMAN NEUROPEPTIDE-Y; PANCREATIC-POLYPEPTIDE; MOLECULAR-STRUCTURE; SECONDARY STRUCTURE; RECEPTOR SUBTYPES; NMR-SPECTROSCOPY; BINDING; EXPRESSION; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Keire, DA Univ Calif Los Angeles, CURE, Digest Dis Res Ctr, Greater Los Angles Vet Hlth Care Syst, Bldg 115,Room 115,11301 Wilshire Blvd, Los Angeles, CA 90073USA Univ Calif Los Angeles Bldg 115,Room 115,11301 Wilshire Blvd Los Angeles CA USA 90073
Citazione:
D.A. Keire et al., "Solution structure of monomeric peptide YY supports the functional significance of the PP-fold", BIOCHEM, 39(32), 2000, pp. 9935-9942

Abstract

Peptide YY (PYY) belongs to a family of peptides including neuropeptide Y (NPY) and pancreatic peptide (PP) that regulate numerous functions through both central and peripheral receptors. The solution structure of these peptides is hypothesized to be critically important in receptor selectivity andactivation, based on prior demonstration of a stable tertiary conformationof PP called the "PP-fold". Circular dichroism (CD) spectra show a pH-dependent structural transition in the pH range 3-4. Thus we describe the tertiary structure of porcine PYY in water at pH 5.5, 25 degrees C, and 150 mM NaCl, as determined from 2D H-1 NMR data recorded at 500 MHz. A constraint set consisting of 396 interproton distances from NOE data was used as input for distance geometry, simulated annealing, and restrained energy minimization calculations in X-PLOR. The RMSDs of the 20 X-PLOR-generated structureswere 0.71 +/- 0.14 and 1.16 +/- 0.17 Angstrom, respectively, for backbone and heavy atom overlays of residues 1-34. The resulting structure consists of two C-terminal helical segments from residues 17 to 22 and 25 to 33 separated by a kink at residues 23, 24, and 25, a turn centered around residues12-14, and the N-terminus folded near residues 30 and 31. The well-definedportions of the PYY structure reported here bear a marked similarity to the structure of PP. Our findings strongly support the importance of the stable folded structure of this family of peptides for binding and activation of Y receptor subtypes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 06:03:53