1l4w

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{{Seed}}
 
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[[Image:1l4w.png|left|200px]]
 
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==NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin==
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The line below this paragraph, containing "STRUCTURE_1l4w", creates the "Structure Box" on the page.
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<StructureSection load='1l4w' size='340' side='right'caption='[[1l4w]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1l4w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [https://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L4W FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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, 1 model</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4w OCA], [https://pdbe.org/1l4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l4w RCSB], [https://www.ebi.ac.uk/pdbsum/1l4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l4w ProSAT]</span></td></tr>
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{{STRUCTURE_1l4w| PDB=1l4w | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l4/1l4w_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1l4w ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of a peptide corresponding to residues 182-202 of the acetylcholine receptor alpha1 subunit in complex with alpha-bungarotoxin was solved using NMR spectroscopy. The peptide contains the complete sequence of the major determinant of AChR involved in alpha-bungarotoxin binding. One face of the long beta hairpin formed by the AChR peptide consists of exposed nonconserved residues, which interact extensively with the toxin. Mutations of these receptor residues confer resistance to the toxin. Conserved AChR residues form the opposite face of the beta hairpin, which creates the inner and partially hidden pocket for acetylcholine. An NMR-derived model for the receptor complex with two alpha-bungarotoxin molecules shows that this pocket is occupied by the conserved alpha-neurotoxin residue R36, which forms cation-pi interactions with both alphaW149 and gammaW55/deltaW57 of the receptor and mimics acetylcholine.
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===NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin===
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The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR.,Samson A, Scherf T, Eisenstein M, Chill J, Anglister J Neuron. 2002 Jul 18;35(2):319-32. PMID:12160749<ref>PMID:12160749</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1l4w" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12160749}}, adds the Publication Abstract to the page
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*[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12160749 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12160749}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1L4W is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4W OCA].
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==Reference==
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The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR., Samson A, Scherf T, Eisenstein M, Chill J, Anglister J, Neuron. 2002 Jul 18;35(2):319-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12160749 12160749]
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[[Category: Bungarus multicinctus]]
[[Category: Bungarus multicinctus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Anglister, J.]]
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[[Category: Torpedo marmorata]]
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[[Category: Eisenstein, M.]]
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[[Category: Anglister J]]
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[[Category: Rodriguez, E.]]
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[[Category: Eisenstein M]]
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[[Category: Samson, A O.]]
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[[Category: Rodriguez E]]
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[[Category: Scherf, T.]]
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[[Category: Samson AO]]
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[[Category: Acetylcholine receptor]]
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[[Category: Scherf T]]
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[[Category: Bungarotoxin]]
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[[Category: Protein-protein complex,intermolecular beta sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:42:28 2008''
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Current revision

NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin

PDB ID 1l4w

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