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| | <StructureSection load='5ebx' size='340' side='right'caption='[[5ebx]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5ebx' size='340' side='right'caption='[[5ebx]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ebx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Black-banded_sea_krait Black-banded sea krait]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EBX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EBX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ebx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Laticauda_semifasciata Laticauda semifasciata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EBX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ebx|3ebx]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ebx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ebx OCA], [http://pdbe.org/5ebx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ebx RCSB], [http://www.ebi.ac.uk/pdbsum/5ebx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ebx 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=5ebx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ebx OCA], [https://pdbe.org/5ebx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ebx RCSB], [https://www.ebi.ac.uk/pdbsum/5ebx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ebx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NXSA_PSSEM NXSA_PSSEM]] Binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs) and with low affinity to neuronal alpha-7 nAChRs and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Blocks the extracellular increase of dopamine evoked by nicotine at 4.2 uM concentrations.<ref>PMID:9305882</ref> <ref>PMID:9840221</ref> | + | [https://www.uniprot.org/uniprot/3S1EA_LATSE 3S1EA_LATSE] Binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs) (tested on Torpedo marmorata, Kd=21 uM) and with low affinity to neuronal alpha-7/CHRNA7 nAChRs (tested on chimeric alpha-7/CHRNA7, Kd=0.07 nM) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission (PubMed:7721859). Blocks the extracellular increase of dopamine evoked by nicotine at 4.2 uM concentrations (PubMed:9840221). In vivo, produces peripheral paralysis.<ref>PMID:7721859</ref> <ref>PMID:9305882</ref> <ref>PMID:9840221</ref> |
| | == 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/eb/5ebx_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eb/5ebx_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Black-banded sea krait]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Corfield, P W.R]] | + | [[Category: Laticauda semifasciata]] |
| - | [[Category: Lee, T J]] | + | [[Category: Corfield PWR]] |
| - | [[Category: Low, B W]] | + | [[Category: Lee T-J]] |
| - | [[Category: Toxin]] | + | [[Category: Low BW]] |
| Structural highlights
Function
3S1EA_LATSE Binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs) (tested on Torpedo marmorata, Kd=21 uM) and with low affinity to neuronal alpha-7/CHRNA7 nAChRs (tested on chimeric alpha-7/CHRNA7, Kd=0.07 nM) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission (PubMed:7721859). Blocks the extracellular increase of dopamine evoked by nicotine at 4.2 uM concentrations (PubMed:9840221). In vivo, produces peripheral paralysis.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of erabutoxin a, a single-chain, 62-residue protein neurotoxin from snake venom, has been determined to 2.0-A resolution by x-ray crystal structure analysis. Molecular replacement methods were used, and the structure refined to a residual R = 0.17. The sites of 62 water molecules and 1 sulfate ion have been located and refined. The structure of erabutoxin a is very similar to that established earlier for erabutoxin b. These toxins from venom of the same snake differ in sequence only at residue 26, which is Asn in erabutoxin a and His in erabutoxin b. The substitution leads to only minor variations in intramolecular hydrogen bonding. Furthermore, the distribution of thermal parameters and the implied regional mobilities are similar in the two structures. In particular, the highly mobile character of the peripheral segment Pro44-Gly49 in both structures supports the specific role proposed for this segment in neurotoxin binding to the acetylcholine receptor. Forty-eight of the solvent sites determined are first surface positions; approximately one-half of these are equivalent to solvent sites in erabutoxin b.
The crystal structure of erabutoxin a at 2.0-A resolution.,Corfield PW, Lee TJ, Low BW J Biol Chem. 1989 Jun 5;264(16):9239-42. PMID:2722828[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tremeau O, Lemaire C, Drevet P, Pinkasfeld S, Ducancel F, Boulain JC, Menez A. Genetic engineering of snake toxins. The functional site of Erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues. J Biol Chem. 1995 Apr 21;270(16):9362-9. PMID:7721859
- ↑ 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
- ↑ 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
- ↑ Corfield PW, Lee TJ, Low BW. The crystal structure of erabutoxin a at 2.0-A resolution. J Biol Chem. 1989 Jun 5;264(16):9239-42. PMID:2722828
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