Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
2005-7-26
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10145-52
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16042391-Amino Acid Sequence, pubmed-meshheading:16042391-Animals, pubmed-meshheading:16042391-Aorta, Thoracic, pubmed-meshheading:16042391-Cobra Venoms, pubmed-meshheading:16042391-Crotalid Venoms, pubmed-meshheading:16042391-Crystallography, X-Ray, pubmed-meshheading:16042391-Cysteine, pubmed-meshheading:16042391-Dose-Response Relationship, Drug, pubmed-meshheading:16042391-Ion Channel Gating, pubmed-meshheading:16042391-Male, pubmed-meshheading:16042391-Membrane Glycoproteins, pubmed-meshheading:16042391-Mice, pubmed-meshheading:16042391-Models, Chemical, pubmed-meshheading:16042391-Models, Molecular, pubmed-meshheading:16042391-Molecular Sequence Data, pubmed-meshheading:16042391-Muscle, Smooth, Vascular, pubmed-meshheading:16042391-Muscle Contraction, pubmed-meshheading:16042391-Potassium Channel Blockers, pubmed-meshheading:16042391-Potassium Channels, Calcium-Activated, pubmed-meshheading:16042391-Solutions
pubmed:year
2005
pubmed:articleTitle
Blocking effect and crystal structure of natrin toxin, a cysteine-rich secretory protein from Naja atra venom that targets the BKCa channel.
pubmed:affiliation
Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230027, China.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't