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 Lettjournal_title
FEBS lettersauthors
Srinivasan KN,Nirthanan S,Sasaki T,Sato K,Cheng B,Gwee MC,Kini RM,Gopalakrishnakone Pdoi
10.1016/s0014-5793(01)02342-0keywords:
subject
Has Abstractpub_date
2001-04-13 00:00:00pages
145-9issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02342-0journal_volume
494pub_type
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