1txb: Difference between revisions
No edit summary |
No edit summary |
||
| (5 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==SOLUTION NMR STRUCTURE OF TOXIN B, A LONG NEUROTOXIN FROM THE VENOM OF THE KING COBRA, 10 STRUCTURES== | ==SOLUTION NMR STRUCTURE OF TOXIN B, A LONG NEUROTOXIN FROM THE VENOM OF THE KING COBRA, 10 STRUCTURES== | ||
<StructureSection load='1txb' size='340' side='right' caption='[[1txb | <StructureSection load='1txb' size='340' side='right'caption='[[1txb]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1txb]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1txb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ophiophagus_hannah Ophiophagus hannah]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TXB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=1txb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txb OCA], [https://pdbe.org/1txb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1txb RCSB], [https://www.ebi.ac.uk/pdbsum/1txb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1txb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/3L22_OPHHA 3L22_OPHHA] Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission.[UniProtKB:P60615] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tx/1txb_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tx/1txb_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <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> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1txb ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 26: | Line 27: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1txb" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Ophiophagus hannah]] | [[Category: Ophiophagus hannah]] | ||
[[Category: Chang | [[Category: Chang C-C]] | ||
[[Category: Jayaraman | [[Category: Jayaraman G]] | ||
[[Category: Kumar | [[Category: Kumar TKS]] | ||
[[Category: Peng | [[Category: Peng S-S]] | ||
[[Category: Yu | [[Category: Yu C]] | ||
Latest revision as of 10:29, 30 October 2024
SOLUTION NMR STRUCTURE OF TOXIN B, A LONG NEUROTOXIN FROM THE VENOM OF THE KING COBRA, 10 STRUCTURESSOLUTION NMR STRUCTURE OF TOXIN B, A LONG NEUROTOXIN FROM THE VENOM OF THE KING COBRA, 10 STRUCTURES
Structural highlights
Function3L22_OPHHA Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission.[UniProtKB:P60615] 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 PubMedThe solution structure of toxin b, a long neurotoxin (73 amino acids and 5 disulfides) from the venom of Ophiophagus hannah (king cobra), has been determined using 1H NMR and dynamical simulated annealing techniques. The structures were calculated using 485 distance constraints and 52 dihedral angle restraints. The 21 structures that were obtained satisfy the experimental restraints and possess good nonbonded contacts. Analysis of the converged structures revealed that the protein consists of a core region from which three finger-like loops extend outwards. The regular secondary structure in toxin b includes a double and a triple stranded antiparallel beta sheet. Comparison with the solution structures of other long neurotoxins reveals that although the structure of toxin b is similar to those of previously reported long neurotoxins, clear local structural differences are observed in regions proposed to be involved in binding to the acetylcholine receptor. A positively charged cluster is found in the C-terminal tail, in Loop III, and in the tip of Loop II. This cationic cluster could be crucial for the binding of the long neurotoxins to the acetylcholine receptor. Solution structure of toxin b, a long neurotoxin from the venom of the king cobra (Ophiophagus hannah).,Peng SS, Kumar TK, Jayaraman G, Chang CC, Yu C J Biol Chem. 1997 Mar 21;272(12):7817-23. PMID:9065446[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
| ||||||||||||||||