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1hc9

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Revision as of 09:38, 22 March 2017

alpha-bungarotoxin complexed with high affinity peptide

Structural highlights

1hc9 is a 4 chain structure with sequence from Bungarus multicinctus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1abt, 1bxp, 1haa, 1haj, 1hn7, 1hoy, 1idg, 1idh, 1idi, 1idl, 2btx
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NXL1V_BUNMU] Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Binds to muscular and neuronal (alpha-7, alpha-8, and alpha-9) nicotinic acetylcholine receptors. [NXL1A_BUNMU] Binds with high affinity to muscular and neuronal (alpha-7, alpha-8, and alpha-9) nicotinic acetylcholine receptors. Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Blocks the extracellular increase of dopamine evoked by nicotine only at the higher dose (4.2 uM).^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Servent D, Winckler-Dietrich V, Hu HY, Kessler P, Drevet P, Bertrand D, Menez A. Only snake curaremimetic toxins with a fifth disulfide bond have high affinity for the neuronal alpha7 nicotinic receptor. J Biol Chem. 1997 Sep 26;272(39):24279-86. PMID:9305882
↑ Dajas-Bailador F, Costa G, Dajas F, Emmett S. Effects of alpha-erabutoxin, alpha-bungarotoxin, alpha-cobratoxin and fasciculin on the nicotine-evoked release of dopamine in the rat striatum in vivo. Neurochem Int. 1998 Oct;33(4):307-12. PMID:9840221
↑ 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. The binding site of acetylcholine receptor as visualized in the X-Ray structure of a complex between alpha-bungarotoxin and a mimotope peptide. Neuron. 2001 Oct 25;32(2):265-75. PMID:11683996

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hc9"

@@ Line 1: / Line 1: @@
 ==alpha-bungarotoxin complexed with high affinity peptide==
 <StructureSection load='1hc9' size='340' side='right' caption='[[1hc9]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1abt|1abt]], [[1bxp|1bxp]], [[1haa|1haa]], [[1haj|1haj]], [[1hn7|1hn7]], [[1hoy|1hoy]], [[1idg|1idg]], [[1idh|1idh]], [[1idi|1idi]], [[1idl|1idl]], [[2btx|2btx]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hc9 OCA], [http://pdbe.org/1hc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hc9 RCSB], [http://www.ebi.ac.uk/pdbsum/1hc9 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hc9 OCA], [http://pdbe.org/1hc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1hc9 RCSB], [http://www.ebi.ac.uk/pdbsum/1hc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1hc9 ProSAT]</span></td></tr>
 </table>
 == Function ==

1hc9

From Proteopedia

Revision as of 09:38, 22 March 2017

alpha-bungarotoxin complexed with high affinity peptide

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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