PDBsum entry 1eyo

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Toxin PDB id
Protein chain
30 a.a.
PDB id:
Name: Toxin
Title: Solution structure of conotoxin tviia from conus tulipa
Structure: Conotoxin tviia. Chain: a. Engineered: yes
Source: Synthetic: yes. Other_details: this peptide was chemically synthesized. This sequence occurs naturally in conus tulipa (tulip cone)
NMR struc: 20 models
Authors: J.M.Hill,P.F.Alewood,D.J.Craik
Key ref:
J.M.Hill et al. (2000). Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three-dimensional solution structure. Eur J Biochem, 267, 4649-4657. PubMed id: 10903497 DOI: 10.1046/j.1432-1327.2000.01507.x
07-May-00     Release date:   06-Sep-00    
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Protein chain
Pfam   ArchSchema ?
P58923  (C7A_CONTU) -  Conotoxin TVIIA
30 a.a.
30 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     pathogenesis   1 term 
  Biochemical function     sodium channel inhibitor activity     1 term  


DOI no: 10.1046/j.1432-1327.2000.01507.x Eur J Biochem 267:4649-4657 (2000)
PubMed id: 10903497  
Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 2. Three-dimensional solution structure.
J.M.Hill, P.F.Alewood, D.J.Craik.
The three-dimensional solution structure of conotoxin TVIIA, a 30-residue polypeptide from the venom of the piscivorous cone snail Conus tulipa, has been determined using 2D 1H NMR spectroscopy. TVIIA contains six cysteine residues which form a 'four-loop' structural framework common to many peptides from Conus venoms including the omega-, delta-, kappa-, and muO-conotoxins. However, TVIIA does not belong to these well-characterized pharmacological classes of conotoxins, but displays high sequence identity with conotoxin GS, a muscle sodium channel blocker from Conus geographus. Structure calculations were based on 562 interproton distance restraints inferred from NOE data, together with 18 backbone and nine side-chain torsion angle restraints derived from spin-spin coupling constants. The final family of 20 structures had mean pairwise rms differences over residues 2-27 of 0.18+/-0.05 A for the backbone atoms and 1.39+/-0.33 A for all heavy atoms. The structure consists of a triple-stranded, antiparallel beta sheet with +2x, -1 topology (residues 7-9, 16-20 and 23-27) and several beta turns. The core of the molecule is formed by three disulfide bonds which form a cystine knot motif common to many toxic and inhibitory polypeptides. The global fold, molecular shape and distribution of amino-acid sidechains in TVIIA is similar to that previously reported for conotoxin GS, and comparison with other four-loop conotoxin structures provides further indication that TVIIA and GS represent a new and distinct subgroup of this structural family. The structure of TVIIA determined in this study provides the basis for determining a structure-activity relationship for these molecules and their interaction with target receptors.
  Selected figure(s)  
Figure 4.
Fig. 4. Comparison of three-dimensional structures of four representative four-loop conotoxins including (from left to right) TVIIA, determined in this study, GS ([44], PDB code 1AG7), a sodium channel blocking peptide, -conotoxin MVIIA ([43], PDB code 1MVI), a calcium channel blocking peptide, and -conotoxin PVIIA ([45], PDB code 1AV3), a potassium channel blocking peptide. (A) Backbone represented as a ribbon with loops 1 and 3 coloured pink, loop 2 green, and loop 4 white. The C-terminal tails of TVIIA and GS are omitted for clarity. (B) Space-filling model of the four peptides with the positively charged residues coloured blue, negative residues red, cysteines yellow, polar residues green and the balance white. The coordinates for PVIIA were kindly provided by M. Scanlon (University of Queensland, Australia).
Figure 5.
Fig. 5. Comparison of conotoxins TVIIA (black) and GS (grey). The molecules are superimposed over the backbone heavy atoms (N, C , C) of residues 2–9, 12–20 and 23–27 of TVIIA and residues 2–9, 12–20 and 26–30 of GS.
  The above figures are reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (2000, 267, 4649-4657) copyright 2000.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
17894348 I.Hudáky, and A.Perczel (2008).
Prolylproline unit in model peptides and in fragments from databases.
  Proteins, 70, 1389-1407.  
15591314 R.Leonard, B.O.Petersen, M.Himly, W.Kaar, N.Wopfner, D.Kolarich, R.van Ree, C.Ebner, J...Duus, F.Ferreira, and F.Altmann (2005).
Two novel types of O-glycans on the mugwort pollen allergen Art v 1 and their role in antibody binding.
  J Biol Chem, 280, 7932-7940.  
14976206 L.Volpon, H.Lamthanh, J.Barbier, N.Gilles, J.Molgó, A.Ménez, and J.M.Lancelin (2004).
NMR solution structures of delta-conotoxin EVIA from Conus ermineus that selectively acts on vertebrate neuronal Na+ channels.
  J Biol Chem, 279, 21356-21366.
PDB codes: 1g1p 1g1z
15044438 N.L.Daly, J.A.Ekberg, L.Thomas, D.J.Adams, R.J.Lewis, and D.J.Craik (2004).
Structures of muO-conotoxins from Conus marmoreus. I nhibitors of tetrodotoxin (TTX)-sensitive and TTX-resistant sodium channels in mammalian sensory neurons.
  J Biol Chem, 279, 25774-25782.
PDB code: 1rmk
12193600 L.A.Miles, C.Y.Dy, J.Nielsen, K.J.Barnham, M.G.Hinds, B.M.Olivera, G.Bulaj, and R.S.Norton (2002).
Structure of a novel P-superfamily spasmodic conotoxin reveals an inhibitory cystine knot motif.
  J Biol Chem, 277, 43033-43040.
PDB code: 1ixt
10903496 J.M.Hill, A.R.Atkins, M.L.Loughnan, A.Jones, D.A.Adams, R.C.Martin, R.J.Lewis, D.J.Craik, and P.F.Alewood (2000).
Conotoxin TVIIA, a novel peptide from the venom of Conus tulipa 1. Isolation, characterization and chemical synthesis.
  Eur J Biochem, 267, 4642-4648.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.