Functional site of bukatoxin, an alpha-type sodium channel neurotoxin from the Chinese scorpion (Buthus martensi Karsch) venom: probable role of the (52)PDKVP(56) loop.

Abstract:

:Alpha-toxins from scorpion venoms prolong the action potential of excitable cells by blocking sodium channel inactivation. We have purified bukatoxin, an alpha-toxin from scorpion (Buthus martensi Karsch) venom, to homogeneity. Bukatoxin produced marked relaxant responses in the carbachol-precontracted rat anococcygeus muscle (ACM), which were mediated through the L-arginine-nitric oxide synthase-nitric oxide pathway, consequent to a neuronal release of nitric oxide. Based on the presence of proline residues in the flanking segments of protein-protein interaction sites, we predicted the site between (52)PP(56) to be the potential interaction site of bukatoxin. A homology model of bukatoxin indicated the presence of this site on the surface. Buka11, a synthetic peptide designed based on this predicted site, produced a concentration-dependent nitric oxide-mediated relaxant response in ACM. Using alanine-substituted peptides, we have shown the importance (53)DKV(55) flanked by proline residues in the functional site of bukatoxin.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Srinivasan KN,Nirthanan S,Sasaki T,Sato K,Cheng B,Gwee MC,Kini RM,Gopalakrishnakone P

doi

10.1016/s0014-5793(01)02342-0

keywords:

subject

Has Abstract

pub_date

2001-04-13 00:00:00

pages

145-9

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02342-0

journal_volume

494

pub_type

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