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1ljz
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ljz]] is a 2 chain structure with sequence 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=1LJZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LJZ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ljz]] is a 2 chain structure with sequence 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=1LJZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LJZ FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l4w|1l4w]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l4w|1l4w]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ljz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ljz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ljz RCSB], [http://www.ebi.ac.uk/pdbsum/1ljz 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=1ljz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ljz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ljz RCSB], [http://www.ebi.ac.uk/pdbsum/1ljz PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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> [[http://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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</StructureSection> | </StructureSection> | ||
[[Category: Bungarus multicinctus]] | [[Category: Bungarus multicinctus]] | ||
| - | [[Category: Anglister, J | + | [[Category: Anglister, J]] |
| - | [[Category: Chill, J H | + | [[Category: Chill, J H]] |
| - | [[Category: Eisenstein, M | + | [[Category: Eisenstein, M]] |
| - | [[Category: Samson, A O | + | [[Category: Samson, A O]] |
| - | [[Category: Scherf, T | + | [[Category: Scherf, T]] |
[[Category: Acetylcholine receptor]] | [[Category: Acetylcholine receptor]] | ||
[[Category: Beta-hairpin]] | [[Category: Beta-hairpin]] | ||
Revision as of 04:39, 25 December 2014
NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin
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