1hc9

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[[Image:1hc9.gif|left|200px]]
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{{STRUCTURE_1hc9| PDB=1hc9 | SCENE= }}
{{STRUCTURE_1hc9| PDB=1hc9 | SCENE= }}
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'''A-BUNGAROTOXIN COMPLEXED WITH HIGH AFFINITY PEPTIDE'''
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===A-BUNGAROTOXIN COMPLEXED WITH HIGH AFFINITY PEPTIDE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11683996 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11683996}}
==About this Structure==
==About this Structure==
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[[Category: Protein-peptide complex]]
[[Category: Protein-peptide complex]]
[[Category: Toxin]]
[[Category: Toxin]]
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Revision as of 04:58, 1 July 2008

Image:1hc9.png

Template:STRUCTURE 1hc9

A-BUNGAROTOXIN COMPLEXED WITH HIGH AFFINITY PEPTIDE

Template:ABSTRACT PUBMED 11683996

About this Structure

1HC9 is a Protein complex structure of sequences from Bungarus multicinctus. Full crystallographic information is available from OCA.

Reference

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 JM, Balass M, Fridkin M, Smit AB, Brejc K, Sixma TK, Katchalski-Katzir E, Sussman JL, Fuchs S, Neuron. 2001 Oct 25;32(2):265-75. PMID:11683996

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