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Titolo:
High-resolution solution structure of gurmarin, a sweet-taste-suppressing plant polypeptide
Autore:
Fletcher, JI; Dingley, AJ; Smith, R; Connor, M; Christie, MJ; King, GF;
Indirizzi:
Univ Sydney, Dept Biochem, Sydney, NSW 2006, Australia Univ Sydney SydneyNSW Australia 2006 iochem, Sydney, NSW 2006, Australia Univ Sydney, Dept Pharmacol, Sydney, NSW 2006, Australia Univ Sydney Sydney NSW Australia 2006 rmacol, Sydney, NSW 2006, Australia Univ Dusseldorf, Inst Phys Biol, D-4000 Dusseldorf, Germany Univ Dusseldorf Dusseldorf Germany D-4000 ol, D-4000 Dusseldorf, Germany Univ Queensland, Dept Biochem, St Lucia, Qld 4067, Australia Univ Queensland St Lucia Qld Australia 4067 St Lucia, Qld 4067, Australia
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 2, volume: 264, anno: 1999,
pagine: 525 - 533
SICI:
0014-2956(199909)264:2<525:HSSOGA>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
FUNNEL-WEB SPIDER; NUCLEAR MAGNETIC-RESONANCE; GATED SODIUM-CHANNEL; AMINO-ACID-SEQUENCE; COUPLING-CONSTANTS; 3-DIMENSIONAL STRUCTURE; DISTANCE GEOMETRY; GYMNEMA-SYLVESTRE; CALCIUM CHANNELS; H-1-NMR SPECTRA;
Keywords:
gurmarin; ion channels; NMR; protein structure; sweet-taste suppression;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: King, GF Univ Connecticut, Ctr Hlth, Dept Biochem, 263 Farmington Ave, Farmington, CT 06032 USA Univ Connecticut 263 Farmington Ave Farmington CT USA06032 2 USA
Citazione:
J.I. Fletcher et al., "High-resolution solution structure of gurmarin, a sweet-taste-suppressing plant polypeptide", EUR J BIOCH, 264(2), 1999, pp. 525-533

Abstract

Gurmarin is a 35-residue polypeptide from the Asclepiad vine Gymnema sylvestre. It has been utilised as a pharmacological tool in the study of sweet-taste transduction because of its ability to selectively inhibit the neuralresponse to sweet tastants in rats. We have chemically synthesised and folded gurmarin and determined its three-dimensional solution structure to high resolution using two-dimensional NMR spectroscopy. Structure calculationsutilised 612 interproton-distance, 19 dihedral-angle, and 18 hydrogen-bondrestraints. The structure is well defined for residues 3-34, with backboneand heavy atom rms differences of 0.27 +/- 0.09 Angstrom and 0.73 +/- 0.09Angstrom, respectively. Gurmarin adopts a compact structure containing an antiparallel beta-hairpin (residues 22-34), several well-defined beta-turns, and a cystine-knot motif commonly observed in toxic and inhibitory polypeptides. Despite striking structural homology with delta-atracotoxin, a spider neurotoxin known to slow the inactivation of voltage-gated Na+ channels,we show that gurmarin has no effect on a variety of voltage-sensitive channels.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 21:27:29