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PDBsum entry 1idh
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protein Protein-protein interface(s) links
Toxin PDB id
1idh

 

 

 

 

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Contents
Protein chains
74 a.a. *
18 a.a. *
* Residue conservation analysis
PDB id:
1idh
Name: Toxin
Title: The nmr solution structure of the complex formed between alpha- bungarotoxin and an 18mer cognate peptide
Structure: Alpha-bungarotoxin. Chain: a. Synonym: long neurotoxin 1. Acetylcholine receptor protein, alpha chain. Chain: b. Synonym: nachr-alpha1-subunit. Engineered: yes
Source: Bungarus multicinctus. Many-banded krait. Organism_taxid: 8616. Other_details: purchased from sigma. Torpedo californica. Pacific electric ray. Organism_taxid: 7787. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 20 models
Authors: H.Zeng,L.Moise,M.A.Grant,E.Hawrot
Key ref:
H.Zeng et al. (2001). The solution structure of the complex formed between alpha-bungarotoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica. J Biol Chem, 276, 22930-22940. PubMed id: 11312275 DOI: 10.1074/jbc.M102300200
Date:
04-Apr-01     Release date:   25-Apr-01    
PROCHECK
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 Headers
 References

Protein chain
P60615  (3L21A_BUNMU) -  Alpha-bungarotoxin from Bungarus multicinctus
Seq:
Struc: 		95 a.a.
74 a.a.
Protein chain
P02710  (ACHA_TETCF) -  Acetylcholine receptor subunit alpha from Tetronarce californica
Seq:
Struc: 		461 a.a.
18 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1074/jbc.M102300200 J Biol Chem 276:22930-22940 (2001)
PubMed id: 11312275  
 
 
The solution structure of the complex formed between alpha-bungarotoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica.
H.Zeng, L.Moise, M.A.Grant, E.Hawrot.
 
  ABSTRACT  
 
The region encompassing residues 181-98 on the alpha1 subunit of the muscle-type nicotinic acetylcholine receptor forms a major determinant for the binding of alpha-neurotoxins. We have prepared an (15)N-enriched 18-amino acid peptide corresponding to the sequence in this region to facilitate structural elucidation by multidimensional NMR. Our aim was to determine the structural basis for the high affinity, stoichiometric complex formed between this cognate peptide and alpha-bungarotoxin, a long alpha-neurotoxin. Resonances in the complex were assigned through heteronuclear and homonuclear NMR experiments, and the resulting interproton distance constraints were used to generate ensemble structures of the complex. Thr(8), Pro(10), Lys(38), Val(39), Val(40), and Pro(69) in alpha-bungarotoxin and Tyr(189), Tyr(190), Thr(191), Cys(192), Asp(195), and Thr(196) in the peptide participate in major intermolecular contacts. A comparison of the free and bound alpha-bungarotoxin structures reveals significant conformational rearrangements in flexible regions of alpha-bungarotoxin, mainly loops I, II, and the C-terminal tail. Furthermore, several of the calculated structures suggest that cation-pi interactions may be involved in binding. The root mean square deviation of the polypeptide backbone in the complex is 2.07 A. This structure provides, to date, the highest resolution description of the contacts between a prototypic alpha-neurotoxin and its cognate recognition sequence.
 
  Selected figure(s)  
 
Figure 8.
Fig. 8. Stereo view of the surface charge profile of the Bgtx· 18-mer complex. Surface charge potentials were calculated as described under "Experimental Procedures." Blue regions show positive charge, and red regions show negative charge. See Fig. 5B for orientation. The figure was prepared using the program MOLMOL (42). 		Figure 9.
Fig. 9. Orientation of a suggested Tyr190-Lys38 cation- interaction. The two side chains are taken from one of the 20 ensemble Bgtx· 18-mer structures depicted in Fig. 5. a, the distance between the NZ of Lys38 and the CE2 of Tyr190 is 5.49 Å; b, the distance between the NZ of Lys38 and the CE1 of Tyr190 is 5.85 Å; c, the distance between the CG of Tyr190 and the NZ of Lys38 is 5.53 Å.
 
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 22930-22940) copyright 2001.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18327915 A.O.Samson, and M.Levitt (2008).
Inhibition mechanism of the acetylcholine receptor by alpha-neurotoxins as revealed by normal-mode dynamics.
  Biochemistry, 47, 4065-4070.  
18508600 G.B.Wells (2008).
Structural answers and persistent questions about how nicotinic receptors work.
  Front Biosci, 13, 5479-5510.  
18035847 S.Flemer, B.M.Lacey, and R.J.Hondal (2008).
Synthesis of peptide substrates for mammalian thioredoxin reductase.
  J Pept Sci, 14, 637-647.  
17651090 D.Kalamida, K.Poulas, V.Avramopoulou, E.Fostieri, G.Lagoumintzis, K.Lazaridis, A.Sideri, M.Zouridakis, and S.J.Tzartos (2007).
Muscle and neuronal nicotinic acetylcholine receptors. Structure, function and pathogenicity.
  FEBS J, 274, 3799-3845.  
14997549 I.Hudáky, Z.Gáspári, O.Carugo, M.Cemazar, S.Pongor, and A.Perczel (2004).
Vicinal disulfide bridge conformers by experimental methods and by ab initio and DFT molecular computations.
  Proteins, 55, 152-168.  
14745112 S.Nirthanan, and M.C.Gwee (2004).
Three-finger alpha-neurotoxins and the nicotinic acetylcholine receptor, forty years on.
  J Pharmacol Sci, 94, 1.  
12885641 H.S.Young, L.G.Herbette, and V.Skita (2003).
Alpha-bungarotoxin binding to acetylcholine receptor membranes studied by low angle X-ray diffraction.
  Biophys J, 85, 943-953.  
12785053 P.Chowdhury, M.Gondry, R.Genet, J.L.Martin, A.Ménez, M.Négrerie, and J.W.Petrich (2003).
Picosecond dynamics of a peptide from the acetylcholine receptor interacting with a neurotoxin probed by tailored tryptophan fluorescence.
  Photochem Photobiol, 77, 151-157.  
12160749 A.Samson, T.Scherf, M.Eisenstein, J.Chill, and J.Anglister (2002).
The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR.
  Neuron, 35, 319-332.
PDB codes: 1l4w 1ljz 1lk1
11867717 C.Fruchart-Gaillard, B.Gilquin, S.Antil-Delbeke, N.Le Novère, T.Tamiya, P.J.Corringer, J.P.Changeux, A.Ménez, and D.Servent (2002).
Experimentally based model of a complex between a snake toxin and the alpha 7 nicotinic receptor.
  Proc Natl Acad Sci U S A, 99, 3216-3221.  
11814338 M.Scarselli, O.Spiga, A.Ciutti, A.Bernini, L.Bracci, B.Lelli, L.Lozzi, D.Calamandrei, D.Di Maro, S.Klein, and N.Niccolai (2002).
NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor.
  Biochemistry, 41, 1457-1463.
PDB codes: 1hoy 1ik8 1ikc 1jbd
11683996 M.Harel, R.Kasher, A.Nicolas, J.M.Guss, M.Balass, M.Fridkin, A.B.Smit, K.Brejc, T.K.Sixma, E.Katchalski-Katzir, J.L.Sussman, and S.Fuchs (2001).
The binding site of acetylcholine receptor as visualized in the X-Ray structure of a complex between alpha-bungarotoxin and a mimotope peptide.
  Neuron, 32, 265-275.
PDB code: 1hc9
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.

 

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