1HC9

alpha-bungarotoxin complexed with high affinity peptide


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.202 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

The Binding Site of Acetylcholine Receptor as Visualized in the X-Ray Structure of a Complex between Alpha-Bungarotoxin and a Mimotope Peptide.

Harel, M.Kasher, R.Nicolas, A.Guss, J.M.Balass, M.Fridkin, M.Smit, A.B.Brejc, K.Sixma, T.K.Katchalski-Katzir, E.Sussman, J.L.Fuchs, S.

(2001) Neuron 32: 265

  • DOI: https://doi.org/10.1016/s0896-6273(01)00461-5
  • Primary Citation of Related Structures:  
    1HC9

  • PubMed Abstract: 

    We have determined the crystal structure at 1.8 A resolution of a complex of alpha-bungarotoxin with a high affinity 13-residue peptide that is homologous to the binding region of the alpha subunit of acetylcholine receptor. The peptide fits snugly to the toxin and adopts a beta hairpin conformation. The structures of the bound peptide and the homologous loop of acetylcholine binding protein, a soluble analog of the extracellular domain of acetylcholine receptor, are remarkably similar. Their superposition indicates that the toxin wraps around the receptor binding site loop, and in addition, binds tightly at the interface of two of the receptor subunits where it inserts a finger into the ligand binding site, thus blocking access to the acetylcholine binding site and explaining its strong antagonistic activity.


  • Organizational Affiliation

    Department of Structural Biology, Weizmann Institute of Science, 76100, Rehovot, Israel.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ALPHA-BUNGAROTOXIN ISOFORM V3174Bungarus multicinctusMutation(s): 0 
UniProt
Find proteins for P60616 (Bungarus multicinctus)
Explore P60616 
Go to UniProtKB:  P60616
Entity Groups  
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UniProt GroupP60616
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
ALPHA-BUNGAROTOXIN ISOFORM A3174Bungarus multicinctusMutation(s): 0 
UniProt
Find proteins for P60615 (Bungarus multicinctus)
Explore P60615 
Go to UniProtKB:  P60615
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UniProt GroupP60615
Sequence Annotations
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  • Reference Sequence

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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
PEPTIDE INHIBITOR
C, D
13synthetic constructMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.235 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.202 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 42.042α = 90
b = 153.356β = 90
c = 73.263γ = 90
Software Package:
Software NamePurpose
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-11-10
    Type: Initial release
  • Version 1.1: 2012-06-20
    Changes: Database references, Derived calculations, Non-polymer description, Other, Refinement description, Source and taxonomy, Structure summary, Version format compliance
  • Version 1.2: 2012-12-19
    Changes: Database references
  • Version 1.3: 2017-03-22
    Changes: Source and taxonomy
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description