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001-es BibID:	BIBFORM050051
Első szerző:	Schwartz, Elisabeth F.
Cím:	OcyKTx2, a new K+-channel toxin characterized from the venom of the scorpion Opisthacanthus cayaporum / Elisabeth F. Schwartz, Adam Bartok, Carlos Alberto Schwartz, Ferenc Papp, Froylan Gomez-Lagunas, Gyorgy Panyi, Lourival D. Possani
Dátum:	2013
Megjegyzések:	Opisthacanthus cayaporum belongs to the Liochelidae family, and the scorpions from this genus occur in southern Africa, Central America and South America and, therefore, can be considered a true Gondwana heritage. In this communication, the isolation, primary structure characterization, and K(+)-channel blocking activity of new peptide from this scorpion venom are reported. OcyKTx2 is a 34 amino acid long peptide with four disulfide bridges and molecular mass of 3807 Da. Electrophysiological assays conducted with pure OcyKTx2 showed that this toxin reversibly blocks Shaker B K(+)-channels with a Kd of 82 nM, and presents an even better affinity toward hKv1.3, blocking it with a Kd of approximately 18 nM. OcyKTx2 shares high sequence identity with peptides belonging to subfamily 6 of alpha-KTxs that clustered very closely in the phylogenetic tree included here. Sequence comparison, chain length and number of disulfide bridges analysis classify OcyKTx2 into subfamily 6 of the alpha-KTx scorpion toxins (systematic name, alpha-KTx6.17)
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban analysis article Brazil Peptides Research Research Support Scorpions Support Toxins
Megjelenés:	Peptides. - 46 (2013), p. 40-46. -
További szerzők:	Bartók Ádám (1984-) (biotechnológus) Schwartz, Carlos Alberto Papp Ferenc (1979-) (biofizikus) Gomez-Lagunas, Froylan Panyi György (1966-) (biofizikus) Possani, Lourival Domingos
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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