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Titolo:
Solution structure of HpTX2, a toxin from Heteropoda venatoria spider thatblocks Kv4.2 potassium channel
Autore:
Bernard, C; Legros, C; Ferrat, G; Bischoff, U; Marquardt, A; Pongs, O; Darbon, H;
Indirizzi:
IFRI, AFMB, CNRS, UPR 9030, F-13402 Marseille 20, France IFRI Marseille France 20 B, CNRS, UPR 9030, F-13402 Marseille 20, France Univ Hamburg, AMNH, Inst Neurale Signalverarbeitung, D-20246 Hamburg, Germany Univ Hamburg Hamburg Germany D-20246 arbeitung, D-20246 Hamburg, Germany GENIONmbH, D-20149 Hamburg, Germany GENIONmbH Hamburg Germany D-20149GENIONmbH, D-20149 Hamburg, Germany
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 11, volume: 9, anno: 2000,
pagine: 2059 - 2067
SICI:
0961-8368(200011)9:11<2059:SSOHAT>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
CA2+-ACTIVATED K+ CHANNELS; KAPPA-CONOTOXIN PVIIA; COUPLING-CONSTANTS; SCORPION TOXIN; CHARYBDOTOXIN; APAMIN; NMR; PEPTIDES; SPECTROSCOPY; POLYPEPTIDE;
Keywords:
heteropodatoxin; NMR; spider toxin; structure determination; voltage-dependent potassium channel;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
41
Recensione:
Indirizzi per estratti:
Indirizzo: Darbon, H IFRI, AFMB, CNRS, UPR 9030, 31 Chemin Jospeh-Aiguier, F-13402 Marseille 20, France IFRI 31 Chemin Jospeh-Aiguier Marseille France 20 le 20, France
Citazione:
C. Bernard et al., "Solution structure of HpTX2, a toxin from Heteropoda venatoria spider thatblocks Kv4.2 potassium channel", PROTEIN SCI, 9(11), 2000, pp. 2059-2067

Abstract

HpTX2 is a toxin from the venom of Heteropoda venatoria spider that has been demonstrated to bind on Kv4.2 potassium channel. We have determined the solution structure of recombinant HpTX2 by use of conventional two-dimensional NMR techniques followed by distance-geometry and molecular dynamics. The calculated structure belongs to the Inhibitory Cystin Knot structural family that consists in a compact disulfide-bonded core, from which four loopsemerge. A poorly defined two-stranded antiparallel beta -sheet (residues 20-23 and 25-28) is detected. Analysis of the electrostatic charge anisotropy allows us to propose a functional map of HpTX2 different from the one described for kappa -conotoxin PVIIA, but strongly related to the one of charybdotoxin. The orientation of the dipole moment of HpTX2 emerges through K27which could therefore be the critical lysine residue. Close to this lysineare a second basic residue, R23, an aromatic cluster (F7, W25, W30) and anhydrophobic side chain (L24). The high density in aromatic side chains of the putative functional surface as well as the lack of an asparagine is proposed to be the structural basis of the specificity of HpTX2 toward Kv4.2 channel.

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Documento generato il 05/12/20 alle ore 14:07:34