Use of Venom Peptides to Probe Ion Channel Structure and Function

被引:128
作者
Dutertre, Sebastien [1 ,2 ]
Lewis, Richard J. [1 ]
机构
[1] Univ Queensland, Inst Mol Biosci, St Lucia, Qld 4067, Australia
[2] Atheris Labs, CH-1233 Bernex Geneva, Switzerland
基金
英国医学研究理事会;
关键词
NICOTINIC ACETYLCHOLINE-RECEPTOR; NEURONAL SODIUM-CHANNELS; ALPHA-CONOTOXIN BINDING; D-ASPARTATE RECEPTOR; II VOLTAGE SENSOR; K+-CHANNEL; POTASSIUM CHANNELS; CRYSTAL-STRUCTURE; HIGH-AFFINITY; CONANTOKIN-G;
D O I
10.1074/jbc.R109.076596
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Venoms of snakes, scorpions, spiders, insects, sea anemones, and cone snails are complex mixtures of mostly peptides and small proteins that have evolved for prey capture and/or defense. These deadly animals have long fascinated scientists and the public. Early studies isolated lethal components in the search for cures and understanding of their mechanisms of action. Ion channels have emerged as targets for many venom peptides, providing researchers highly selective and potent molecular probes that have proved invaluable in unraveling ion channel structure and function. This minireview highlights molecular details of their toxin-receptor interactions and opportunities for development of peptide therapeutics.
引用
收藏
页码:13315 / 13320
页数:6
相关论文
共 91 条
[1]   κM-conotoxin RIIIK, structural and functional novelty in a K+ channel antagonist [J].
Al-Sabi, A ;
Lennartz, D ;
Ferber, M ;
Gulyas, J ;
Rivier, JEF ;
Olivera, BM ;
Carlomagno, T ;
Terlau, H .
BIOCHEMISTRY, 2004, 43 (27) :8625-8635
[2]   THE NMR SOLUTION STRUCTURE OF A KUNITZ-TYPE PROTEINASE-INHIBITOR FROM THE SEA-ANEMONE STICHODACTYLA-HELIANTHUS [J].
ANTUCH, W ;
BERNDT, KD ;
CHAVEZ, MA ;
DELFIN, J ;
WUTHRICH, K .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1993, 212 (03) :675-684
[3]   A δ-conotoxin from Conus ermineus venom inhibits inactivation in vertebrate neuronal Na+ channels but not in skeletal and cardiac muscles [J].
Barbier, J ;
Lamthanh, H ;
Le Gall, F ;
Favreau, P ;
Benoit, E ;
Chen, HJ ;
Gilles, N ;
Ilan, N ;
Heinemann, SH ;
Gordon, D ;
Ménez, A ;
Molgó, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (06) :4680-4685
[4]   Interaction of SNX482 with domains III and IV inhibits activation gating of α1E (CaV2.3) calcium channels [J].
Bourinet, E ;
Stotz, SC ;
Spaetgens, RL ;
Dayanithi, G ;
Lemos, J ;
Nargeot, J ;
Zamponi, GW .
BIOPHYSICAL JOURNAL, 2001, 81 (01) :79-88
[5]   Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors [J].
Brejc, K ;
van Dijk, WJ ;
Klaassen, RV ;
Schuurmans, M ;
van der Oost, J ;
Smit, AB ;
Sixma, TK .
NATURE, 2001, 411 (6835) :269-276
[6]   δ-conotoxin structure/function through a cladistic analysis [J].
Bulaj, G ;
DeLaCruz, R ;
Azimi-Zonooz, A ;
West, P ;
Watkins, M ;
Yoshikami, D ;
Olivera, BM .
BIOCHEMISTRY, 2001, 40 (44) :13201-13208
[7]   SELECTIVE BLOCKAGE OF VOLTAGE-DEPENDENT K+ CHANNELS BY A NOVEL SCORPION TOXIN [J].
CARBONE, E ;
WANKE, E ;
PRESTIPINO, G ;
POSSANI, LD ;
MAELICKE, A .
NATURE, 1982, 296 (5852) :90-91
[8]   STRUCTURE AND FUNCTION OF VOLTAGE-GATED ION CHANNELS [J].
CATTERALL, WA .
ANNUAL REVIEW OF BIOCHEMISTRY, 1995, 64 :493-531
[9]   Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an α-conotoxin PnIA variant [J].
Celie, PHN ;
Kasheverov, IE ;
Mordvintsev, DY ;
Hogg, RC ;
van Nierop, P ;
van Elk, R ;
van Rossum-Fikkert, SE ;
Zhmak, MN ;
Bertrand, D ;
Tsetlin, V ;
Sixma, TK ;
Smit, AB .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2005, 12 (07) :582-588
[10]   Structure and function of the voltage sensor of sodium channels probed by a β-scorpion toxin [J].
Cestele, Sandrine ;
Yarov-Yarovoy, Vladimir ;
Qu, Yusheng ;
Sampieri, Francois ;
Scheuer, Todd ;
Catterall, William A. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (30) :21332-21344