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( T o p )
1
H y p e r v a r i a b i l i t y
2
D i s u l f i d e c o n n e c t i v i t i e s
3
T y p e s a n d b i o l o g i c a l a c t i v i t i e s
T o g g l e T y p e s a n d b i o l o g i c a l a c t i v i t i e s s u b s e c t i o n
3 . 1
A l p h a
3 . 2
D e l t a , k a p p a , a n d o m e g a
3 . 3
Mu
4
S e e a l s o
5
R e f e r e n c e s
6
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E d i t l i n k s
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A p p e a r a n c e
F r o m W i k i p e d i a , t h e f r e e e n c y c l o p e d i a
This article
is missing information about genetic and architectural classification (ConoServer and PMC4278219).
Please expand the article to include this information. Further details may exist on the talk page . (April 2019 )
Alpha conotoxin precursor
Toxin_8
PF07365
IPR009958
PDOC60004
1mii / SCOPe / SUPFAM
148
1akg
RCSB PDB ; PDBe ; PDBj
structure summary
Conotoxin
PF02950
IPR004214
2cco / SCOPe / SUPFAM
112
1fyg
RCSB PDB ; PDBe ; PDBj
structure summary
A conotoxin is one of a group of neurotoxic peptides isolated from the venom of the marine cone snail , genus Conus .
Conotoxins, which are peptides consisting of 10 to 30 amino acid residues, typically have one or more disulfide bonds . Conotoxins have a variety of mechanisms of actions, most of which have not been determined. However, it appears that many of these peptides modulate the activity of ion channels .[1]
Over the last few decades conotoxins have been the subject of pharmacological interest.[2]
The LD 50 of conotoxin ranges from 5-25 μg/kg.[3] [4] [5]
Hypervariability [ edit ]
Conotoxins are hypervariable even within the same species. They do not act within a body where they are produced (endogenously ) but act on other organisms.[6] Therefore, conotoxin genes experience less selection against mutations (like gene duplication and nonsynonymous substitution ), and mutations remain in the genome longer, allowing more time for potentially beneficial novel functions to arise.[7] Variability in conotoxin components reduces the likelihood that prey organisms will develop resistance; thus cone snails are under constant selective pressure to maintain polymorphism in these genes because failing to evolve and adapt will lead to extinction (Red Queen hypothesis ).[8]
Disulfide connectivities [ edit ]
Types of conotoxins also differ in the number and pattern of disulfide bonds.[9] The disulfide bonding network, as well as specific amino acids in inter-cysteine loops, provide the specificity of conotoxins.[10]
Types and biological activities [ edit ]
The number of conotoxins whose activities have been determined so far is five, and they are called the α(alpha)-, δ(delta)-, κ(kappa)-, μ(mu )-, and ω(omega)- types. Each of the five types of conotoxins attacks a different target:
Alpha conotoxins have two types of cysteine arrangements,[18] and are competitive nicotinic acetylcholine receptor antagonists.
Delta, kappa, and omega [ edit ]
Omega, delta and kappa families of conotoxins have a knottin or inhibitor cystine knot scaffold. The knottin scaffold is a very special disulfide-through-disulfide knot, in which the III-VI disulfide bond crosses the macrocycle formed by two other disulfide bonds (I-IV and II-V) and the interconnecting backbone segments, where I-VI indicates the six cysteine residues starting from the N-terminus. The cysteine arrangements are the same for omega, delta and kappa families, even though omega conotoxins are calcium channel blockers, whereas delta conotoxins delay the inactivation of sodium channels, and kappa conotoxins are potassium channel blockers.[9]
nmr solution structure of piiia toxin, nmr, 20 structures
Mu-conotoxin
PF05374
CL0083
IPR008036
1gib / SCOPe / SUPFAM
112
1ag7
RCSB PDB ; PDBe ; PDBj
structure summary
Mu-conotoxins have two types of cysteine arrangements, but the knottin scaffold is not observed.[19] Mu-conotoxins target the muscle-specific voltage-gated sodium channels,[9] and are useful probes for investigating voltage-dependent sodium channels of excitable tissues.[19] [20] Mu-conotoxins target the voltage-gated sodium channels, preferentially those of skeletal muscle ,[21] and are useful probes for investigating voltage-dependent sodium channels of excitable tissues .[22]
Different subtypes of voltage-gated sodium channels are found in different tissues in mammals, e.g., in muscle and brain, and studies have been carried out to determine the sensitivity and specificity of the mu-conotoxins for the different isoforms.[23]
See also [ edit ]
References [ edit ]
^ Olivera BM, Teichert RW (2007). "Diversity of the neurotoxic Conus peptides: a model for concerted pharmacological discovery" . Molecular Interventions . 7 (5 ): 251–60. doi :10.1124/mi.7.5.7 . PMID 17932414 .
^ "Archived copy" (PDF) . Archived (PDF) from the original on 2017-08-29. Retrieved 2017-03-31 .{{cite web }}
: CS1 maint: archived copy as title (link )
^ "Biological Agent Reference Sheet - Conotoxin" (PDF) . Emory University.
^ Baker, A.L. "toxin ld50 list" . PhycoKey .
^ Olivera BM, Watkins M, Bandyopadhyay P, Imperial JS, de la Cotera EP, Aguilar MB, Vera EL, Concepcion GP, Lluisma A (September 2012). "Adaptive radiation of venomous marine snail lineages and the accelerated evolution of venom peptide genes" . Ann. N. Y. Acad. Sci . 1267 (1 ): 61–70. Bibcode :2012NYASA1267...61O . doi :10.1111/j.1749-6632.2012.06603.x . PMC 3488454 . PMID 22954218 .
^ Wong ES, Belov K (March 2012). "Venom evolution through gene duplications". Gene . 496 (1 ): 1–7. doi :10.1016/j.gene.2012.01.009 . PMID 22285376 .
^ Liow LH, Van Valen L, Stenseth NC (July 2011). "Red Queen: from populations to taxa and communities". Trends Ecol. Evol . 26 (7 ): 349–58. doi :10.1016/j.tree.2011.03.016 . PMID 21511358 .
^ a b c Jones RM, McIntosh JM (2001). "Cone venom--from accidental stings to deliberate injection". Toxicon . 39 (10 ): 1447–1451. doi :10.1016/S0041-0101(01 )00145-3 . PMID 11478951 .
^ Sato K, Kini RM, Gopalakrishnakone P, Balaji RA, Ohtake A, Seow KT, Bay BH (2000). "lambda-conotoxins, a new family of conotoxins with unique disulfide pattern and protein folding. Isolation and characterization from the venom of Conus marmoreus" . J. Biol. Chem . 275 (50 ): 39516–39522. doi :10.1074/jbc.M006354200 . PMID 10988292 .
^ Nicke A, Wonnacott S, Lewis RJ (2004). "Alpha-conotoxins as tools for the elucidation of structure and function of neuronal nicotinic acetylcholine receptor subtypes" . Eur. J. Biochem . 271 (12 ): 2305–2319. doi :10.1111/j.1432-1033.2004.04145.x . PMID 15182346 .
^ Leipold E, Hansel A, Olivera BM, Terlau H, Heinemann SH (2005). "Molecular interaction of delta-conotoxins with voltage-gated sodium channels" . FEBS Lett . 579 (18 ): 3881–3884. doi :10.1016/j.febslet.2005.05.077 . PMID 15990094 .
^ Shon KJ, Stocker M, Terlau H, Stühmer W, Jacobsen R, Walker C, Grilley M, Watkins M, Hillyard DR, Gray WR, Olivera BM (1998). "kappa-Conotoxin PVIIA is a peptide inhibiting the shaker K+ channel" . J. Biol. Chem . 273 (1 ): 33–38. doi :10.1074/jbc.273.1.33 . PMID 9417043 .
^ Li RA, Tomaselli GF (2004). "Using the deadly mu-conotoxins as probes of voltage-gated sodium channels" . Toxicon . 44 (2 ): 117–122. doi :10.1016/j.toxicon.2004.03.028 . PMC 2698010 . PMID 15246758 .
^ Nielsen KJ, Schroeder T, Lewis R (2000). "Structure-activity relationships of omega-conotoxins at N-type voltage-sensitive calcium channels" . J. Mol. Recognit . 13 (2 ): 55–70. doi :10.1002/(SICI)1099-1352(200003/04)13:2<55::AID-JMR488>3.0.CO;2-O . PMID 10822250 . Archived from the original (abstract) on 2011-08-13.
^ Bowersox SS, Luther R (1998). "Pharmacotherapeutic potential of omega-conotoxin MVIIA (SNX-111), an N-type neuronal calcium channel blocker found in the venom of Conus magus". Toxicon . 36 (11 ): 1651–1658. doi :10.1016/S0041-0101(98 )00158-5 . PMID 9792182 .
^ Prommer E (2006). "Ziconotide: a new option for refractory pain". Drugs Today . 42 (6 ): 369–78. doi :10.1358/dot.2006.42.6.973534 . PMID 16845440 .
^ Gray WR, Olivera BM, Zafaralla GC, Ramilo CA, Yoshikami D, Nadasdi L, Hammerland LG, Kristipati R, Ramachandran J, Miljanich G (1992). "Novel alpha- and omega-conotoxins from Conus striatus venom". Biochemistry . 31 (41 ): 11864–11873. doi :10.1021/bi00156a009 . PMID 1390774 .
^ a b Nielsen KJ, Watson M, Adams DJ, Hammarström AK, Gage PW, Hill JM, Craik DJ, Thomas L, Adams D, Alewood PF, Lewis RJ (July 2002). "Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of persistent tetrodotoxin-sensitive sodium channels" (PDF) . J. Biol. Chem . 277 (30 ): 27247–55. doi :10.1074/jbc.M201611200 . PMID 12006587 .
^ Zeikus RD, Gray WR, Cruz LJ, Olivera BM, Kerr L, Moczydlowski E, Yoshikami D (1985). "Conus geographus toxins that discriminate between neuronal and muscle sodium channels" . J. Biol. Chem . 260 (16 ): 9280–8. doi :10.1016/S0021-9258(17 )39364-X . PMID 2410412 .
^ McIntosh JM, Jones RM (October 2001). "Cone venom--from accidental stings to deliberate injection". Toxicon . 39 (10 ): 1447–51. doi :10.1016/S0041-0101(01 )00145-3 . PMID 11478951 .
^ Cruz LJ, Gray WR, Olivera BM, Zeikus RD, Kerr L, Yoshikami D, Moczydlowski E (August 1985). "Conus geographus toxins that discriminate between neuronal and muscle sodium channels" . J. Biol. Chem . 260 (16 ): 9280–8. doi :10.1016/S0021-9258(17 )39364-X . PMID 2410412 .
^ Floresca CZ (2003). "A comparison of the mu-conotoxins by [3H]saxitoxin binding assays in neuronal and skeletal muscle sodium channel" . Toxicol Appl Pharmacol . 190 (2 ): 95–101. doi :10.1016/s0041-008x(03 )00153-4 . PMID 12878039 .
External links [ edit ]
Conotoxins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Baldomero "Toto" Olivera's Short Talk. "Conus Peptides" .
Kaas Q, Westermann JC, Halai R, Wang CK, Craik DJ. "ConoServer" . Institute of Molecular Bioscience, The University of Queensland, Australia. Retrieved 2009-06-02 . A database for conopeptide sequences and structures
Protein folding
Structure determination methods
Globin fold
Homeodomain fold
Alpha solenoid
Death fold
Beta barrel
Beta-propeller
Beta helix
Leucine-rich repeat
Flavodoxin fold
Rossmann fold
Thioredoxin fold
Trefoil knot fold
Ferredoxin fold
Ribonuclease A
SH2-like fold
cytotoxin
enterotoxin
hemotoxin
hepatotoxin
neurotoxin
phototoxin
B
botulinum
Listeriolysin O
Exfoliatin
Toxic shock syndrome toxin
Staphylococcal Enterotoxin B (SEB)
Diphtheria toxin
E. coli heat-stable enterotoxin
Cholera toxin /Heat-labile enterotoxin
Pertussis toxin
Pseudomonas exotoxin
Extracellular adenylate cyclase
type II
type III
Bacillus thuringiensis delta endotoxin
Other B. thuringiensis toxins
Fibronectin binding protein A
Amatoxin (alpha-amanitin , beta-amanitin , gamma-amanitin , epsilon-amanitin )
beta-Nitropropionic acid
Citrinin
Cytochalasin
Ergotamine
Fumonisin (Fumonisin B1 , Fumonisin B2 , Fumonisin B3, Fumonisin B4 )
Gliotoxin
Ibotenic acid
Lolitrem B
Muscimol
Orellanine
Ochratoxin
Patulin
Phalloidin
Sterigmatocystin
Trichothecene
Vomitoxin
Zeranol
Zearalenone
Anisatin
Antiarin
Brucine
Chaconine
Cicutoxin
Coniine
Daphnin
Delphinine
Divicine
Djenkolic acid
Falcarinol
Gossypol
Helenalin
Ledol
Linamarin
Lotaustralin
Mimosine
Oenanthotoxin
Oleandrin
Persin
Protoanemonin
Pseudaconitine
Retronecine
Resiniferatoxin
Scopolamine
Solamargine
Solanidine
Solanine
Solasodamine
Solasodine
Solasonine
Solauricidine
Solauricine
Strychnine
Swainsonine
Tagetitoxin
Tinyatoxin
Tomatine
Toxalbumin
Tutin
Agitoxin
Margatoxin
Slotoxin
Scyllatoxin
Hefutoxin
HgeTx1
HsTx1
Lq2
Birtoxin
Bestoxin
BmKAEP
Phaiodotoxin
Imperatoxin
Pi3
CSTX
Cupiennins
PhTx3
Stromatoxin
Vanillotoxin
Huwentoxin
Eledoisin
Onchidal
Saxitoxin
Tetrodotoxin
Batrachotoxin
Bufotoxins
Epibatidine
Histrionicotoxin
Pumiliotoxin 251D
Samandarin
Samandaridine
Tarichatoxin
Zetekitoxin AB
Beta-Bungarotoxin
Calciseptine
Taicatoxin
Calcicludine
Cardiotoxin III
note: some toxins are produced by lower species and pass through intermediate species
Cronidipine
Darodipine
Dexniguldipine
Elgodipine
Elnadipine
Felodipine
Flordipine
Furnidipine
Iganidipine
Isradipine
Lacidipine
Lemildipine
Lercanidipine
Levamlodipine
Levniguldipine
Manidipine
Mepirodipine
Mesudipine
Nicardipine
Nifedipine
Niguldipine
Niludipine
Nilvadipine
Nimodipine
Nisoldipine
Nitrendipine
Olradipine
Oxodipine
Palonidipine
Pranidipine
Ryodipine (riodipine)
Sagandipine
Sornidipine
Teludipine
Tiamdipine
Trombodipine
Vatanidipine ; Diltiazem derivatives: Clentiazem
Diltiazem
Iprotiazem
Nictiazem
Siratiazem ; Phenylalkylamines : Anipamil
Dagapamil
Devapamil
Dexverapamil
Emopamil
Etripamil
Falipamil
Gallopamil
Levemopamil
Nexopamil
Norverapamil
Ronipamil
Tiapamil
Verapamil ; Others: AH-1058
Brinazarone
Budiodarone
Celivarone
Cyproheptadine
Dronedarone
Fantofarone
SR-33805
Tetrahydropalmatine
Azimilide
Bretylium
Bunaftine
Charybdotoxin
Clamikalant
Conotoxins
Dalazatide
Dendrotoxin
Dofetilide
Dronedarone
E-4031
Hanatoxin
HgeTx1
HsTx1
Ibutilide
Inakalant
Kaliotoxin
Linopirdine
Lolitrem B
Maurotoxin
Nifekalant
Notoxin
Paxilline
Pinokalant
Quinidine
ShK-186
Sotalol
Tedisamil
Terikalant
Tetraethylammonium
Vernakalant
Retigabine
IRKs Tooltip Inwardly rectifying potassium channel
Glibenclamide (glyburide)
Glibornuride
Glicaramide
Gliclazide
Glimepiride
Glipizide
Gliquidone
Glisoxepide
Glyclopyramide
Glycyclamide
Metahexamide
Mitiglinide
Nateglinide
Repaglinide
Tolazamide
Tolbutamide
Bimakalim
Cromakalim
Diazoxide
Emakalim
Levcromakalim
Mazokalim
Minoxidil
Minoxidil sulfate
Naminidil
Nicorandil
Pinacidil
Rilmakalim
Sarakalim
K Ca Tooltip Calcium-activated potassium channel
Meclofenamic acid
Niflumic acid
Nimesulide
Rottlerin (mallotoxin)
Tolfenamic acid
K2Ps Tooltip Tandem pore domain potassium channel
Norfluoxetine
Dronedarone
Encainide
Flecainide
Lidocaine
Lorajmine
Lorcainide
Mexiletine
Moricizine
Pilsicainide
Prajmaline
Procainamide
Propafenone
Quinidine
Sparteine
Tocainide
Atracotoxins (ω-Atracotoxin , Robustoxin , Versutoxin )
Batrachotoxin
Ciguatoxins
Grayanotoxins
Poneratoxin
ENaC Tooltip Epithelial sodium channel
ASICs Tooltip Acid-sensing ion channel
Ibuprofen
PcTX1
Furosemide
Glibenclamide
Mefloquine
Mibefradil
Niflumic acid
CFTR Tooltip Cystic fibrosis transmembrane conductance regulator
1,10-Phenanthroline
4,7-Phenanthroline
7,8-Benzoquinoline
Ivacaftor
Phenanthridine
Mefenamic acid
Mepacrine
Niflumic acid
Talniflumate
Tolfenamic acid
Trifluoperazine
TRPs Tooltip Transient receptor potential channels
LGICs Tooltip Ligand gated ion channels
nAChRs Tooltip Nicotinic acetylcholine receptors
A-366,833
A-582,941
A-867,744
ABT-202
ABT-418
ABT-560
ABT-894
Acetylcholine
Altinicline
Anabasine
Anatabine
Anatoxin-a
AR-R17779
Bephenium hydroxynaphthoate
Butinoline
Butyrylcholine
Carbachol
Choline
Cotinine
Cytisine
Decamethonium
Desformylflustrabromine
Dianicline
Dimethylphenylpiperazinium
Epibatidine
Epiboxidine
Ethanol (alcohol)
Ethoxysebacylcholine
EVP-4473
EVP-6124
Galantamine
GTS-21
Ispronicline
Ivermectin
JNJ-39393406
Levamisole
Lobeline
MEM-63,908 (RG-3487)
Morantel
Nicotine (tobacco )
NS-1738
PHA-543,613
PHA-709,829
PNU-120,596
PNU-282,987
Pozanicline
Pyrantel
Rivanicline
RJR-2429
Sazetidine A
SB-206553
Sebacylcholine
SIB-1508Y
SIB-1553A
SSR-180,711
Suberyldicholine
Suxamethonium (succinylcholine)
Suxethonium (succinyldicholine)
TC-1698
TC-1734
TC-1827
TC-2216
TC-5214
TC-5619
TC-6683
Tebanicline
Tribendimidine
Tropisetron
UB-165
Varenicline
WAY-317,538
XY-4083
18-MC
α-Neurotoxins (e.g., α-bungarotoxin , α-cobratoxin , α-conotoxin , many others)
ABT-126
Alcuronium
Allopregnanolone
Amantadine
Anatruxonium
AQW051
Atracurium
Barbiturates (e.g., pentobarbital , sodium thiopental )
BNC-210
Bungarotoxins (e.g., α-bungarotoxin , κ-bungarotoxin )
Bupropion
BW284C51
BW-A444
Candocuronium iodide (chandonium iodide)
Chlorisondamine
Cisatracurium
Coclaurine
Coronaridine
Curare
Cyclopropane
Dacuronium bromide
Decamethonium
Dehydronorketamine
Desflurane
Dextromethorphan
Dextropropoxyphene
Dextrorphan
Diadonium
DHβE
Dihydrochandonium
Dimethyltubocurarine (metocurine)
Dioscorine
Dipyrandium
Dizocilpine (MK-801)
Doxacurium
Encenicline
Enflurane
Erythravine
Esketamine
Fazadinium
Gallamine
Gantacurium chloride
Halothane
Hexafluronium
Hexamethonium (benzohexonium)
Hydroxybupropion
Hydroxynorketamine
Ibogaine
Isoflurane
Ketamine
Kynurenic acid
Laudanosine
Laudexium (laudolissin)
Levacetylmethadol
Levomethadone
Malouetine
ME-18-MC
Mecamylamine
Memantine
Methadone
Methorphan (racemethorphan)
Methyllycaconitine
Metocurine
Mivacurium
Morphanol (racemorphan)
Neramexane
Nitrous oxide
Norketamine
Pancuronium bromide
Pempidine
Pentamine
Pentolinium
Phencyclidine
Pipecuronium bromide
Progesterone
Promegestone
Radafaxine
Rapacuronium bromide
Reboxetine
Rocuronium bromide
Sevoflurane
Stercuronium iodide
Surugatoxin
Thiocolchicoside
Threohydrobupropion
Toxiferine
Tramadol
Trimetaphan camsilate (trimethaphan camsylate)
Tropeinium
Tubocurarine
Vanoxerine
Vecuronium bromide
Xenon
Adafenoxate
Choline (lecithin )
Citicoline
Cyprodenate
Dimethylethanolamine
Glycerophosphocholine
Meclofenoxate (centrophenoxine)
Phosphatidylcholine
Phosphatidylethanolamine
Phosphorylcholine
Pirisudanol
Muscarinic acetylcholine receptor modulators
Acetylcholine metabolism/transport modulators
R e t r i e v e d f r o m " https://en.wikipedia.org/w/index.php?title=Conotoxin&oldid=1183872786 "
C a t e g o r i e s :
● S n a i l t o x i n s
● I o n c h a n n e l t o x i n s
● N e u r o t o x i n s
● N i c o t i n i c a n t a g o n i s t s
● P e r i p h e r a l m e m b r a n e p r o t e i n s
H i d d e n c a t e g o r i e s :
● C S 1 m a i n t : a r c h i v e d c o p y a s t i t l e
● A r t i c l e s w i t h s h o r t d e s c r i p t i o n
● S h o r t d e s c r i p t i o n i s d i f f e r e n t f r o m W i k i d a t a
● A r t i c l e s t o b e e x p a n d e d f r o m A p r i l 2 0 1 9
● T h i s p a g e w a s l a s t e d i t e d o n 7 N o v e m b e r 2 0 2 3 , a t 0 0 : 5 4 ( U T C ) .
● T e x t i s a v a i l a b l e u n d e r t h e C r e a t i v e C o m m o n s A t t r i b u t i o n - S h a r e A l i k e L i c e n s e 4 . 0 ;
a d d i t i o n a l t e r m s m a y a p p l y . B y u s i n g t h i s s i t e , y o u a g r e e t o t h e T e r m s o f U s e a n d P r i v a c y P o l i c y . W i k i p e d i a ® i s a r e g i s t e r e d t r a d e m a r k o f t h e W i k i m e d i a F o u n d a t i o n , I n c . , a n o n - p r o f i t o r g a n i z a t i o n .
● P r i v a c y p o l i c y
● A b o u t W i k i p e d i a
● D i s c l a i m e r s
● C o n t a c t W i k i p e d i a
● C o d e o f C o n d u c t
● D e v e l o p e r s
● S t a t i s t i c s
● C o o k i e s t a t e m e n t
● M o b i l e v i e w