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Peptide record

TPDB29902

Neurotoxin Toxicity standard
47 amino acids
Basic Information
3D PDB MODEL
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TPDB29902
Neurotoxin Toxicity
Toxicity and safety peptides
NTxPred2 Peptipedia
standard
No
A 47-aa standard natural multi-activity (Neurotoxin and Toxicity) peptide sequence curated from NTxPred2 and Peptipedia, with an available 3D structural model.
Sequence
DLRQCTRNAPGSTWGRCCLNPMCGNFCCPRSGCTCAYNWRRGIYCSC
Physicochemical Analysis
C215H332N72O63S11
EHKV
C
5286.11
8.32
6
1
11
+5
-0.55
-0.389
29.15
Mammalian: 1.1 hour Yeast: 3 min E.coli: >10 hour
14605
276.29
23
Residue Composition
number
2
A
6
R
4
N
1
D
10
C
0
E
1
Q
5
G
0
H
1
I
2
L
0
K
1
M
1
F
3
P
3
S
3
T
2
W
2
Y
0
V
Amino Acid Distribution
A: 2 R: 6 N: 4 D: 1 C: 10 E: 0 Q: 1 G: 5 H: 0 I: 1 L: 2 K: 0 M: 1 F: 1 P: 3 S: 3 T: 3 W: 2 Y: 2 V: 0
Chemical Descriptors
47
C215H332N72O63S11
5286.11
8.32
+5
-0.55
-0.389
Evidence Records 1 records
Evidence 1 Activity

Activity

Neurotoxin
FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Through its two C-terminal domains, this homodimeric protein would bind to two nAChR allosteric sites, located outside the nAChR C-loop of the principal binding face and at the adjacent binding interface in a clockwise direction (By similarity). This toxin specifically blocks mammalian neuronal nAChR of the alpha-7/CHRNA7, alpha-3-beta-2/CHRNA3-CHRNB2 and alpha-4-beta-2/CHRNA4-CHRNB2 subtypes (PubMed:16790424). VxXXA and VxXXB inhibit alpha-7/CHRNA7 and alpha-3-beta-2/CHRNA3-CHRNB2 nAChR more efficiently than VxXXC (PubMed:16790424). VxXXB is the most effective at inhibiting alpha-4-beta-2/CHRNA4-CHRNB2 nAChR, followed by VxXXC and VxXXA (PubMed:16790424). {ECO:0000250|UniProtKB:P0C1W6, ECO:0000269|PubMed:16790424}.

Target

nicotinic acetylcholine receptor (nAChR) acetylcholine receptor

Source & Reference

NA
UniProtKB/Swiss-Prot Tox-Prot

Other

Conus vexillum (Flag cone)
Neurotoxin Postsynaptic neurotoxin Acetylcholine receptor inhibiting toxin Ion channel impairing toxin
Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Through its two C-terminal domains, this homodimeric protein would bind to two nAChR allosteric sites, located outside the nAChR C-loop of the principal binding face and at the adjacent binding interface in a clockwise direction (By similarity).
Alpha-conotoxin VxXXC (VxXIIC)
cone snail
Conotoxin D superfamily
Evidence at protein level
Acetylcholine receptor inhibiting toxin Direct protein sequencing Disulfide bond Hydroxylation Ion channel impairing toxin Neurotoxin Postsynaptic neurotoxin Secreted Toxin
TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305|PubMed:16790424}.
Additional Detail Fields 7 fields
Acetylcholine receptor inhibiting toxin Direct protein sequencing Disulfide bond Hydroxylation Ion channel impairing toxin Neurotoxin Postsynaptic neurotoxin Secreted Toxin
Neurotoxin Postsynaptic neurotoxin Acetylcholine receptor inhibiting toxin Ion channel impairing toxin
Evidence at protein level
Conotoxin D superfamily
Alpha-conotoxin VxXXC (VxXIIC)
TISSUE SPECIFICITY: Expressed by the venom duct. {ECO:0000305|PubMed:16790424}.
cone snail