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1jbd

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Revision as of 08:43, 17 January 2018

NMR Structure of the Complex Between alpha-bungarotoxin and a Mimotope of the Nicotinic Acetylcholine Receptor

Structural highlights

1jbd is a 2 chain structure with sequence from Bungarus multicinctus. This structure supersedes the now removed PDB entry 1hn7. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1hn7, 1hoy, 1ik8, 1ikc
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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).^[1] ^[2]

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

A combinatorial library approach was used to produce synthetic peptides mimicking the snake neurotoxin binding site of nicotinic receptors. Among the sequences, which inhibited binding of alpha-bungarotoxin to muscle and neuronal nicotinic receptors, HRYYESSLPWYPD, a 14-amino acid peptide with considerably higher toxin-binding affinity than the other synthesized peptides, was selected, and the structure of its complex with the toxin was analyzed by NMR. Comparison of the solution structure of the free toxin and its complex with this peptide indicated that complex formation induced extensive conformational rearrangements mainly at finger II and the carboxy terminus of the protein. The peptidyl residues P10 and Y4 seemed to be critical for peptide folding and complex stability, respectively. The latter residue of the peptide strongly interacted with the protein by entering a small pocket delimited by D30, C33, S34, R36, and V39 toxin side chains.

NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor.,Scarselli M, Spiga O, Ciutti A, Bernini A, Bracci L, Lelli B, Lozzi L, Calamandrei D, Di Maro D, Klein S, Niccolai N Biochemistry. 2002 Feb 5;41(5):1457-63. PMID:11814338^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ Scarselli M, Spiga O, Ciutti A, Bernini A, Bracci L, Lelli B, Lozzi L, Calamandrei D, Di Maro D, Klein S, Niccolai N. NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor. Biochemistry. 2002 Feb 5;41(5):1457-63. PMID:11814338

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/1jbd"

@@ Line 1: / Line 1: @@
 ==NMR Structure of the Complex Between alpha-bungarotoxin and a Mimotope of the Nicotinic Acetylcholine Receptor==
 <StructureSection load='1jbd' size='340' side='right' caption='[[1jbd]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1jbd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hn7 1hn7]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JBD FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hn7|1hn7]], [[1hoy|1hoy]], [[1ik8|1ik8]], [[1ikc|1ikc]]</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=1jbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jbd OCA], [http://pdbe.org/1jbd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jbd RCSB], [http://www.ebi.ac.uk/pdbsum/1jbd 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=1jbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jbd OCA], [http://pdbe.org/1jbd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jbd RCSB], [http://www.ebi.ac.uk/pdbsum/1jbd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jbd ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 12: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/1jbd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/1jbd_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 27: / Line 28: @@
 </div>
 <div class="pdbe-citations 1jbd" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Bungarotoxin|Bungarotoxin]]
 == References ==
 <references/>

1jbd

From Proteopedia

Revision as of 08:43, 17 January 2018

NMR Structure of the Complex Between alpha-bungarotoxin and a Mimotope of the Nicotinic Acetylcholine Receptor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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