1txb: Difference between revisions

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<StructureSection load='1txb' size='340' side='right'caption='[[1txb]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='1txb' size='340' side='right'caption='[[1txb]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1txb]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TXB FirstGlance]. <br>
<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1txa|1txa]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1txa|1txa]]</div></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=1txb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1txb OCA], [http://pdbe.org/1txb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1txb RCSB], [http://www.ebi.ac.uk/pdbsum/1txb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1txb 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=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 ==
[[http://www.uniprot.org/uniprot/NXL2_OPHHA NXL2_OPHHA]] Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Binds to muscular and neuronal (only alpha-7 alpha-8 alpha-9) nicotinic acetylcholine receptors (By similarity).  
[[https://www.uniprot.org/uniprot/NXL2_OPHHA NXL2_OPHHA]] Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Binds to muscular and neuronal (only alpha-7 alpha-8 alpha-9) nicotinic acetylcholine receptors (By similarity).  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 12:33, 29 September 2021

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

1txb is a 1 chain structure with sequence from Ophiophagus hannah. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NXL2_OPHHA] Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Binds to muscular and neuronal (only alpha-7 alpha-8 alpha-9) nicotinic acetylcholine receptors (By similarity).

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 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

  1. Peng SS, Kumar TK, Jayaraman G, Chang CC, Yu C. Solution structure of toxin b, a long neurotoxin from the venom of the king cobra (Ophiophagus hannah). J Biol Chem. 1997 Mar 21;272(12):7817-23. PMID:9065446
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