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7qpu
From Proteopedia
(Difference between revisions)
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==Botulinum neurotoxin A5 cell binding domain in complex with GM1b oligosaccharide== | ==Botulinum neurotoxin A5 cell binding domain in complex with GM1b oligosaccharide== | ||
| - | <StructureSection load='7qpu' size='340' side='right'caption='[[7qpu]]' scene=''> | + | <StructureSection load='7qpu' size='340' side='right'caption='[[7qpu]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7qpu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QPU FirstGlance]. <br> |
| - | </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=7qpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpu OCA], [https://pdbe.org/7qpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpu RCSB], [https://www.ebi.ac.uk/pdbsum/7qpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpu ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene></td></tr> |
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] </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=7qpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qpu OCA], [https://pdbe.org/7qpu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qpu RCSB], [https://www.ebi.ac.uk/pdbsum/7qpu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qpu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Botulinum neurotoxins (BoNT) cause the potentially fatal neuroparalytic disease botulism that arises due to proteolysis of a SNARE protein. Each BoNT is comprised of three domains: a cell binding domain (HC), a translocation domain (HN), and a catalytic (Zn(2+) endopeptidase) domain (LC). The HC is responsible for neuronal specificity by targeting both a protein and ganglioside receptor at the neuromuscular junction. Although highly toxic, some BoNTs are commercially available as therapeutics for the treatment of a range of neuromuscular conditions. Here we present the crystal structures of two BoNT cell binding domains, HC/A4 and HC/A5, in a complex with the oligosaccharide of ganglioside, GD1a and GM1b, respectively. These structures, along with a detailed comparison with the previously reported apo-structures, reveal the conformational changes that occur upon ganglioside binding and the interactions involved. | ||
| + | |||
| + | Crystal Structures of Botulinum Neurotoxin Subtypes A4 and A5 Cell Binding Domains in Complex with Receptor Ganglioside.,Gregory KS, Mojanaga OO, Liu SM, Acharya KR Toxins (Basel). 2022 Feb 8;14(2). pii: toxins14020129. doi:, 10.3390/toxins14020129. PMID:35202156<ref>PMID:35202156</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7qpu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bontoxilysin]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Acharya | + | [[Category: Acharya, K R]] |
| - | [[Category: Gregory | + | [[Category: Gregory, K S]] |
| - | [[Category: Liu | + | [[Category: Liu, S M]] |
| + | [[Category: Cell binding domain]] | ||
| + | [[Category: Neurotoxin]] | ||
| + | [[Category: Oligosaccharide]] | ||
| + | [[Category: Receptor]] | ||
| + | [[Category: Toxin]] | ||
Revision as of 07:21, 16 March 2022
Botulinum neurotoxin A5 cell binding domain in complex with GM1b oligosaccharide
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