6f0p
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Botulinum neurotoxin A4 Hc domain== | |
| + | <StructureSection load='6f0p' size='340' side='right' caption='[[6f0p]], [[Resolution|resolution]] 1.34Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6f0p]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F0P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F0P FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=6f0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f0p OCA], [http://pdbe.org/6f0p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f0p RCSB], [http://www.ebi.ac.uk/pdbsum/6f0p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f0p ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Clostridium botulinum neurotoxins (BoNTs) cause the life-threatening condition, botulism. However, while they have the potential to cause serious harm, they are increasingly being utilised for therapeutic applications. BoNTs comprise of seven distinct serotypes termed BoNT/A through BoNT/G, with the most widely characterised being sub-serotype BoNT/A1. Each BoNT consists of three structurally distinct domains, a binding domain (HC), a translocation domain (HN), and a proteolytic domain (LC). The HC domain is responsible for the highly specific targeting of the neurotoxin to neuronal cell membranes. Here, we present two high-resolution structures of the binding domain of subtype BoNT/A3 (HC/A3) and BoNT/A4 (HC/A4) at 1.6A and 1.34A resolution, respectively. The structures of both proteins share a high degree of similarity to other known BoNT HC domains whilst containing some subtle differences, and are of benefit to research into therapeutic neurotoxins with novel characteristics. | ||
| - | + | High resolution crystal structures of Clostridium botulinum neurotoxin A3 and A4 binding domains.,Davies JR, Rees J, Liu SM, Acharya KR J Struct Biol. 2017 Dec 26. pii: S1047-8477(17)30233-2. doi:, 10.1016/j.jsb.2017.12.010. PMID:29288126<ref>PMID:29288126</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6f0p" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acharya, K R]] | ||
| + | [[Category: Davies, J R]] | ||
| + | [[Category: Liu, S M]] | ||
[[Category: Rees, J]] | [[Category: Rees, J]] | ||
| - | [[Category: | + | [[Category: A4]] |
| - | [[Category: | + | [[Category: Binding domain]] |
| + | [[Category: Botulinum neurotoxin a4 subtype]] | ||
| + | [[Category: Hc domain]] | ||
| + | [[Category: Toxin]] | ||
Revision as of 08:33, 10 January 2018
Botulinum neurotoxin A4 Hc domain
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