1qkd

From Proteopedia

(Difference between revisions)

Revision as of 06:32, 9 August 2023

ERABUTOXIN

Structural highlights

1qkd is a 2 chain structure with sequence from Laticauda semifasciata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.49Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Erabutoxin a has been crystallized in its monomeric and dimeric forms. The structures were refined at 1.50 and 1.49 A resolution, respectively, using synchrotron radiation data. The crystals belong to space group P212121, with cell dimensions a = 49.84, b = 46.62, c = 21.22 A for the monomer and a = 55.32, b = 53.54, c = 40.76 A for the dimer. Using starting models from earlier structure determinations, the monomeric structure refined to an R value of 16.7% (8004 unique reflections, 17.0-1.50 A resolution range), while the dimeric structure has been solved by the molecular-replacement method with a final R value of 16.9% (19 444 unique reflections, 17.4-1.49 A resolution range). The high-resolution electron-density maps clearly revealed significant discrete disorder in the proteins and allowed an accurate determination of the solvent structure. For the monomer, the side chains of six residues were modelled with alternate conformers and 106 sites for water molecules and one site for a sulfate ion were included in the final model, whereas for the dimer, 206 sites for water molecules were included and both C-terminal residues together with the side chains of 11 residues adopted alternative conformations. A comparison was made with earlier structure determinations. The features of the solvent structure of the erabutoxin molecules are discussed in detail.

Structure of dimeric and monomeric erabutoxin a refined at 1.5 A resolution.,Nastopoulos V, Kanellopoulos PN, Tsernoglou D Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):964-74. PMID:9757111^[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
↑ Nastopoulos V, Kanellopoulos PN, Tsernoglou D. Structure of dimeric and monomeric erabutoxin a refined at 1.5 A resolution. Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):964-74. PMID:9757111

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qkd"

Categories: Large Structures | Laticauda semifasciata | Kanellopoulos PN | Nastopoulos V | Tsernoglou D

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1qkd]] is a 2 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=1QKD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QKD FirstGlance]. <br>
-</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=1qkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qkd OCA], [https://pdbe.org/1qkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qkd RCSB], [https://www.ebi.ac.uk/pdbsum/1qkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qkd ProSAT]</span></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]] 1.49&#8491;</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=1qkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qkd OCA], [https://pdbe.org/1qkd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qkd RCSB], [https://www.ebi.ac.uk/pdbsum/1qkd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qkd ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 34: @@
 [[Category: Large Structures]]
 [[Category: Laticauda semifasciata]]
-[[Category: Kanellopoulos, P N]]
+[[Category: Kanellopoulos PN]]
-[[Category: Nastopoulos, V]]
+[[Category: Nastopoulos V]]
-[[Category: Tsernoglou, D]]
+[[Category: Tsernoglou D]]
-[[Category: Erabutoxin]]
-[[Category: Neurotoxin]]

1qkd

From Proteopedia

Revision as of 06:32, 9 August 2023

ERABUTOXIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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