6thy

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'''Unreleased structure'''
 
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The entry 6thy is ON HOLD until Paper Publication
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==Botulinum neurotoxin A3 Hc domain in complex with GD1a==
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<StructureSection load='6thy' size='340' side='right'caption='[[6thy]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6thy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6THY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6THY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f0o|6f0o]], [[2vu9|2vu9]], [[5tpc|5tpc]]</td></tr>
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<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=6thy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6thy OCA], [http://pdbe.org/6thy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6thy RCSB], [http://www.ebi.ac.uk/pdbsum/6thy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6thy ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Botulinum neurotoxins (BoNTs) are one of the most toxic proteins known to humans. Their molecular structure is comprised of three essential domains - a cell binding domain (HC ), translocation domain (HN ), and catalytic domain (LC). The HC domain facilitates the highly specific binding of BoNTs to the neuronal membrane via a dual-receptor complex involving a protein receptor and a ganglioside. Variation in activity/toxicity across subtypes of serotype A has been attributed to changes in protein and ganglioside interactions and their implications are important in the design of novel BoNT-based therapeutics. Here, we present the structure of BoNT/A3 cell binding domain (HC /A3) in complex with the ganglioside GD1a at 1.75 A resolution. The structure revealed that six residues interact with the three outermost monosaccharides of GD1a through several key hydrogen bonding interactions. A detailed comparison of structures of HC /A3 with HC /A1 revealed subtle conformational differences at the ganglioside binding site (GBS) upon carbohydrate binding.
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Authors:
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Crystal structure of botulinum neurotoxin subtype A3 cell binding domain in complex with GD1a co-receptor ganglioside.,Gregory KS, Liu SM, Acharya KR FEBS Open Bio. 2020 Jan 16. doi: 10.1002/2211-5463.12790. PMID:31945264<ref>PMID:31945264</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6thy" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Acharya, K R]]
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[[Category: Gregory, K S]]
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[[Category: Liu, S M]]
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[[Category: Botulinum]]
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[[Category: Ganglioside]]
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[[Category: Gd1a]]
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[[Category: Neurotoxin]]
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[[Category: Toxin]]

Revision as of 15:43, 29 January 2020

Botulinum neurotoxin A3 Hc domain in complex with GD1a

PDB ID 6thy

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