1ljz

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==NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin==
==NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin==
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<StructureSection load='1ljz' size='340' side='right'caption='[[1ljz]], [[NMR_Ensembles_of_Models | 19 NMR models]]' scene=''>
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<StructureSection load='1ljz' size='340' side='right'caption='[[1ljz]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ljz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LJZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ljz]] 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=1LJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LJZ FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1l4w|1l4w]]</div></td></tr>
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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, 19 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ljz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ljz OCA], [https://pdbe.org/1ljz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ljz RCSB], [https://www.ebi.ac.uk/pdbsum/1ljz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ljz ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ljz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ljz OCA], [https://pdbe.org/1ljz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ljz RCSB], [https://www.ebi.ac.uk/pdbsum/1ljz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ljz ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
 
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[[https://www.uniprot.org/uniprot/NXL1A_BUNMU 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).<ref>PMID:9305882</ref> <ref>PMID:9840221</ref> [[https://www.uniprot.org/uniprot/ACHA_TORMA ACHA_TORMA]] After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
 
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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<jmolCheckbox>
<jmolCheckbox>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lj/1ljz_consurf.spt"</scriptWhenChecked>
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lj/1ljz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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[[Category: Bungarus multicinctus]]
[[Category: Bungarus multicinctus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Anglister, J]]
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[[Category: Torpedo marmorata]]
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[[Category: Chill, J H]]
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[[Category: Anglister J]]
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[[Category: Eisenstein, M]]
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[[Category: Chill JH]]
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[[Category: Samson, A O]]
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[[Category: Eisenstein M]]
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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: Beta-hairpin]]
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[[Category: Bungarotoxin]]
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[[Category: Intermolecular beta-sheet]]
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[[Category: Receptor]]
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[[Category: Toxin]]
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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 1ljz

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