Function and solution structure of huwentoxin-X, a specific blocker of   N-type calcium channels, from the Chinese bird spider Ornithoctonus   huwena

doi:10.1074/jbc.M513542200

CORC > 北京大学 > 生命科学学院

	Function and solution structure of huwentoxin-X, a specific blocker of N-type calcium channels, from the Chinese bird spider Ornithoctonus huwena
	Li, ZH ; Dai, J ; Dai, LJ ; Deng, MC ; Zhu, Z ; Hu, WJ ; Liang, SP
刊名	journal of biological chemistry
	2006
关键词	OMEGA-CONOTOXIN GVIA SELENOCOSMIA-HUWENA CA2+ CHANNELS HAINANTOXIN-IV PEPTIDE TOXINS VENOM AFFINITY RELEASE ANTINOCICEPTION IDENTIFICATION
DOI	10.1074/jbc.M513542200
英文摘要	Huwentoxin-X (HWTX-X) is a novel peptide toxin, purified from the venom of the spider Ornithoctonus huwena. It comprises 28 amino acid residues including six cysteine residues as disulfide bridges linked in the pattern of I - IV, II - V, and III - VI. Its cDNA, determined by rapid amplification of 3' and 5' cDNA ends, encodes a 65-residue prepropeptide. HWTX-X shares low sequence homology with omega-conotoxins GVIA and MVIIA, two well known blockers of N-type Ca2+ channels. Nevertheless, whole cell studies indicate that it can block N-type Ca2+ channels in rat dorsal root ganglion cells (IC50 40 nM) and the blockage by HWTX-X is completely reversible. The rank order of specificity for N-type Ca2+ channels is GVIA approximate to HWTX- X > MVIIA. In contrast to GVIA and MVIIA, HWTX- X had no detectable effect on the twitch response of rat vas deferens to low frequency electrical stimulation, indicating that HWTX- X has different selectivity for isoforms of N-type Ca2+ channels, compared with GVIA or MVIIA. A comparison of the structures of HWTX- X and GVIA reveals that they not only adopt a common structural motif ( inhibitor cystine knot), but also have a similar functional motif, a binding surface formed by the critical residue Tyr, and several basic residues. However, the dissimilarities of their binding surfaces provide some insights into their different selectivities for isoforms of N-type Ca2+ channels.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000236247100040&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Biochemistry & Molecular Biology; SCI(E); EI; PubMed; 2; ARTICLE; 13; 8628-8635; 281
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/346121]
专题	生命科学学院
推荐引用方式 GB/T 7714	Li, ZH,Dai, J,Dai, LJ,et al. Function and solution structure of huwentoxin-X, a specific blocker of N-type calcium channels, from the Chinese bird spider Ornithoctonus huwena[J]. journal of biological chemistry,2006.
APA	Li, ZH.,Dai, J.,Dai, LJ.,Deng, MC.,Zhu, Z.,...&Liang, SP.(2006).Function and solution structure of huwentoxin-X, a specific blocker of N-type calcium channels, from the Chinese bird spider Ornithoctonus huwena.journal of biological chemistry.
MLA	Li, ZH,et al."Function and solution structure of huwentoxin-X, a specific blocker of N-type calcium channels, from the Chinese bird spider Ornithoctonus huwena".journal of biological chemistry (2006).