1hc9
From Proteopedia
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| - | [[Image:1hc9.gif|left|200px]]<br /> | + | [[Image:1hc9.gif|left|200px]]<br /><applet load="1hc9" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hc9" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1hc9, resolution 1.8Å" /> | caption="1hc9, resolution 1.8Å" /> | ||
'''A-BUNGAROTOXIN COMPLEXED WITH HIGH AFFINITY PEPTIDE'''<br /> | '''A-BUNGAROTOXIN COMPLEXED WITH HIGH AFFINITY PEPTIDE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HC9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] with IOD as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 1HC9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] with IOD as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC2:Ido Binding Site For Chain B'>AC2</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HC9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:15:52 2007'' |
Revision as of 14:06, 18 December 2007
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A-BUNGAROTOXIN COMPLEXED WITH HIGH AFFINITY PEPTIDE
Overview
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.
About this Structure
1HC9 is a Protein complex structure of sequences from Bungarus multicinctus with IOD as ligand. Known structural/functional Site: . 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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