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Titolo:
CONFORMATIONAL-ANALYSIS OF A TOXIC PEPTIDE FROM TRIMERESURUS-WAGLERI WHICH BLOCKS THE NICOTINIC ACETYLCHOLINE-RECEPTOR
Autore:
SELLIN LC; MATTILA K; ANNILA A; SCHMIDT JJ; MCARDLE JJ; HYVONEN M; RANTALA TT; KIVISTO T;
Indirizzi:
OULU UNIV,DEPT PHYS SCI,DIV BIOPHYS SF-90570 OULU FINLAND OULU UNIV,DEPT PHYS SCI,DIV PHYS SF-90570 OULU FINLAND CHEM TECHNOL STATE TECH RES CTR FINLAND SF-02150 ESPOO FINLAND USA,MED RES INST INFECT DIS,DIV TOXICOL FREDERICK MD 21702 UNIV MED & DENT NEW JERSEY,NEW JERSEY MED SCH,DEPT PHARMACOL & TOXICOL NEWARK NJ 07103
Titolo Testata:
Biophysical journal
fascicolo: 1, volume: 70, anno: 1996,
pagine: 3 - 13
SICI:
0006-3495(1996)70:1<3:COATPF>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
LETHAL PEPTIDES; PIT VIPER; VENOM; DYNAMICS; MUSCLE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
L.C. Sellin et al., "CONFORMATIONAL-ANALYSIS OF A TOXIC PEPTIDE FROM TRIMERESURUS-WAGLERI WHICH BLOCKS THE NICOTINIC ACETYLCHOLINE-RECEPTOR", Biophysical journal, 70(1), 1996, pp. 3-13

Abstract

The 22-residue toxic peptide (WTX1) from the venom of the Southeast Asian snake Trimeresurus wagleri has multiple sites of action, but its lethal effect has been attributed to blocking the postsynaptic acetylcholine receptor at the neuromuscular junction. The 3-dimensional structure of WTX1 was studied using 2-dimensional nuclear magnetic resonance spectroscopy, circular dichroism, and computer simulations, In aqueous solution, WTX1 was shown to have extended and flexible ''tails'' defined by a short, rigid disulfide-bonded loop. The flexible regions can undergo structural rearrangement when moved from an aqueous to a less polar environment and may contribute to its effectiveness at different receptor sites, By substituting Gly or Phe for His at position 10, significant effects on the disulfide bond formation and, thereby, the activity of the peptide were observed, These results suggest that evensubtle differences in single residues can have profound effects on the dynamics of folding, disulfide bond formation, and activity of this toxic peptide.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 12:37:53