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[[Image:1idh.png|left|200px]]


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==THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE==
The line below this paragraph, containing "STRUCTURE_1idh", creates the "Structure Box" on the page.
<StructureSection load='1idh' size='340' side='right'caption='[[1idh]]' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1idh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [https://en.wikipedia.org/wiki/Tetronarce_californica Tetronarce californica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDH FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HSL:HOMOSERINE+LACTONE'>HSL</scene></td></tr>
{{STRUCTURE_1idh|  PDB=1idh  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1idh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idh OCA], [https://pdbe.org/1idh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1idh RCSB], [https://www.ebi.ac.uk/pdbsum/1idh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1idh ProSAT]</span></td></tr>
 
</table>
===THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE===
== Function ==
 
[https://www.uniprot.org/uniprot/3L21A_BUNMU 3L21A_BUNMU] Binds with high affinity to muscular (tested on Torpedo marmorata, Kd=0.4 nM) and neuronal (tested on chimeric alpha-7/CHRNA7, Kd=0.95 nM) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission (PubMed:9305882). It also shows an activity on GABA(A) receptors (PubMed:16549768, PubMed:25634239). It antagonises GABA-activated currents with high potency when tested on primary hippocampal neurons (PubMed:25634239). It inhibits recombinantly expressed GABA(A) receptors composed of alpha-2-beta-2-gamma-2 (GABRA2-GABRB2-GABRG2) subunits with high potency (62.3% inhibition at 20 uM of toxin) (PubMed:25634239). It also shows a weaker inhibition on GABA(A) receptors composed of alpha-1-beta-2-gamma-2 (GABRA1-GABRB2-GABRG2) subunits, alpha-4-beta-2-gamma-2 (GABRA4-GABRB2-GABRG2) subunits, and alpha-5-beta-2-gamma-2 (GABRA5-GABRB2-GABRG2) subunits (PubMed:25634239). A very weak inhibition is also observed on GABA(A) receptor composed of alpha-1-beta-3-gamma-2 (GABRA1-GABRB3-GABRG2) (PubMed:26221036). It has also been shown to bind and inhibit recombinant GABA(A) receptor beta-3/GABRB3 subunit (Kd=about 50 nM) (PubMed:16549768). In addition, it blocks the extracellular increase of dopamine evoked by nicotine only at the higher dose (4.2 uM) (PubMed:9840221).<ref>PMID:16549768</ref> <ref>PMID:25634239</ref> <ref>PMID:9305882</ref> <ref>PMID:9840221</ref>
 
== Evolutionary Conservation ==
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==About this Structure==
  </jmolCheckbox>
[[1idh]] is a 2 chain structure of [[Bungarotoxin]] with sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDH OCA].  
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1idh ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Bungarotoxin]]
*[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:11312275</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Bungarus multicinctus]]
[[Category: Bungarus multicinctus]]
[[Category: Torpedo californica]]
[[Category: Large Structures]]
[[Category: Grant, M A.]]
[[Category: Tetronarce californica]]
[[Category: Hawrot, E.]]
[[Category: Grant MA]]
[[Category: Moise, L.]]
[[Category: Hawrot E]]
[[Category: Zeng, H.]]
[[Category: Moise L]]
[[Category: Alpha 1 subunit]]
[[Category: Zeng H]]
[[Category: Alpha-bungarotoxin]]
[[Category: Cation-pi interaction]]
[[Category: Nicotinic acetylcholine receptor]]
[[Category: Nmr]]
[[Category: Protein-protein interaction]]

Latest revision as of 10:46, 3 April 2024

THE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDETHE NMR SOLUTION STRUCTURE OF THE COMPLEX FORMED BETWEEN ALPHA-BUNGAROTOXIN AND AN 18MER COGNATE PEPTIDE

Structural highlights

1idh is a 2 chain structure with sequence from Bungarus multicinctus and Tetronarce californica. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

3L21A_BUNMU Binds with high affinity to muscular (tested on Torpedo marmorata, Kd=0.4 nM) and neuronal (tested on chimeric alpha-7/CHRNA7, Kd=0.95 nM) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission (PubMed:9305882). It also shows an activity on GABA(A) receptors (PubMed:16549768, PubMed:25634239). It antagonises GABA-activated currents with high potency when tested on primary hippocampal neurons (PubMed:25634239). It inhibits recombinantly expressed GABA(A) receptors composed of alpha-2-beta-2-gamma-2 (GABRA2-GABRB2-GABRG2) subunits with high potency (62.3% inhibition at 20 uM of toxin) (PubMed:25634239). It also shows a weaker inhibition on GABA(A) receptors composed of alpha-1-beta-2-gamma-2 (GABRA1-GABRB2-GABRG2) subunits, alpha-4-beta-2-gamma-2 (GABRA4-GABRB2-GABRG2) subunits, and alpha-5-beta-2-gamma-2 (GABRA5-GABRB2-GABRG2) subunits (PubMed:25634239). A very weak inhibition is also observed on GABA(A) receptor composed of alpha-1-beta-3-gamma-2 (GABRA1-GABRB3-GABRG2) (PubMed:26221036). It has also been shown to bind and inhibit recombinant GABA(A) receptor beta-3/GABRB3 subunit (Kd=about 50 nM) (PubMed:16549768). In addition, it blocks the extracellular increase of dopamine evoked by nicotine only at the higher dose (4.2 uM) (PubMed:9840221).[1] [2] [3] [4]

Evolutionary Conservation

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

See Also

References

  1. ↑ McCann CM, Bracamontes J, Steinbach JH, Sanes JR. The cholinergic antagonist alpha-bungarotoxin also binds and blocks a subset of GABA receptors. Proc Natl Acad Sci U S A. 2006 Mar 28;103(13):5149-54. doi:, 10.1073/pnas.0600847103. Epub 2006 Mar 20. PMID:16549768 doi:http://dx.doi.org/10.1073/pnas.0600847103
  2. ↑ Hannan S, Mortensen M, Smart TG. Snake neurotoxin alpha-bungarotoxin is an antagonist at native GABA(A) receptors. Neuropharmacology. 2015 Jun;93:28-40. doi: 10.1016/j.neuropharm.2015.01.001. Epub, 2015 Jan 26. PMID:25634239 doi:http://dx.doi.org/10.1016/j.neuropharm.2015.01.001
  3. ↑ 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
  4. ↑ 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
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