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1lxh
From Proteopedia
(Difference between revisions)
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<StructureSection load='1lxh' size='340' side='right'caption='[[1lxh]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='1lxh' size='340' side='right'caption='[[1lxh]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1lxh]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1lxh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_kaouthia Naja kaouthia] and [https://en.wikipedia.org/wiki/Pacific_electric_ray Pacific electric ray]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LXH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LXH FirstGlance]. <br> |
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HSL:HOMOSERINE+LACTONE'>HSL</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HSL:HOMOSERINE+LACTONE'>HSL</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lxg|1lxg]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lxg|1lxg]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lxh OCA], [https://pdbe.org/1lxh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lxh RCSB], [https://www.ebi.ac.uk/pdbsum/1lxh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lxh ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/NXL1_NAJKA NXL1_NAJKA]] The monomeric form binds with high affinity to muscular, Torpedo (muscle-type), and neuronal alpha-7 nicotinic acetylcholine receptors (nAChR). Has no effect on alpha-3/beta-2 nAChR. Causes paralysis by preventing acetylcholine binding to the nAChR. Does not show any blockade of the nicotine-evoked release of dopamine and does not affect ACh release. In mice lung cancer, causes reduction of tumor growth.<ref>PMID:18381281</ref> <ref>PMID:6771288</ref> <ref>PMID:6553056</ref> <ref>PMID:2086254</ref> <ref>PMID:9053737</ref> <ref>PMID:9305882</ref> <ref>PMID:9840221</ref> <ref>PMID:10574958</ref> <ref>PMID:18067132</ref> The homodimeric form binds with low affinity to Torpedo (muscle-type) and alpha-7 nAChRs, whereas it acquires the capacity to block alpha-3/beta-2 nAChRs.<ref>PMID:18381281</ref> <ref>PMID:6771288</ref> <ref>PMID:6553056</ref> <ref>PMID:2086254</ref> <ref>PMID:9053737</ref> <ref>PMID:9305882</ref> <ref>PMID:9840221</ref> <ref>PMID:10574958</ref> <ref>PMID:18067132</ref> [[https://www.uniprot.org/uniprot/ACHA_TORCA ACHA_TORCA]] 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]] | ||
Revision as of 06:50, 18 August 2021
Solution structure of alpha-cobratoxin complexed with a cognate peptide (minimized average structure)
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