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Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from naja atra venom that targets the BKCa channel

Academic Article
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Overview

authors

  • Wang, J.
  • Guo, Min
  • Lou, X. H.
  • Duan, Y. Y.
  • Cheng, X. P.
  • Teng, M. K.
  • Niu, L. W.
  • Liu, Q.
  • Huang, Q. Q.
  • Hao, Q.
  • Shen, B.

publication date

  • August 2005

journal

  • Biochemistry  Journal

abstract

  • Cysteine-rich secretory proteins (CRISPs) are widespread in snake venoms. Some members of these CRISPs recently have been found to block L-type Ca(2+) channels or cyclic nucleotide-gated ion (CNG) channels. Here, natrin purified from Naja atra venom, a member of the CRISP family, can induce a further contractile response in the endothelium-denuded thoracic aorta of mouse which has been contracted by a high-K(+) solution. Further experiments show it can block the high-conductance calcium-activated potassium (BK(Ca)) channel in a concentration-dependent manner with an IC(50) of 34.4 nM and a Hill coefficient of 1.02, which suggests that only a single natrin molecule is required to bind an ion channel to block BK(Ca) current. The crystal structure of natrin displaying two domains in tandem shows its cysteine-rich domain (CRD) has relatively independent flexibility, especially for the C-terminal long loop (loop I) of CRD to participate in the interface of two domains. On the basis of previous studies of CNG channel and L-Ca(2+) channel blockers, and the sequence and structural comparison of natrin and stecrisp, the deviation of the vital loop I of CRD is suggested to contribute to different effects of some CRISPs in protein-protein interaction.

subject areas

  • Amino Acid Sequence
  • Animals
  • Aorta, Thoracic
  • Cobra Venoms
  • Crotalid Venoms
  • Crystallography, X-Ray
  • Cysteine
  • Dose-Response Relationship, Drug
  • Ion Channel Gating
  • Male
  • Membrane Glycoproteins
  • Mice
  • Models, Chemical
  • Models, Molecular
  • Molecular Sequence Data
  • Muscle Contraction
  • Muscle, Smooth, Vascular
  • Potassium Channel Blockers
  • Potassium Channels, Calcium-Activated
  • Solutions
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi050614m

PubMed ID

  • 16042391
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Additional Document Info

start page

  • 10145

end page

  • 10152

volume

  • 44

issue

  • 30

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