7qpu: Difference between revisions
New page: '''Unreleased structure''' The entry 7qpu is ON HOLD Authors: Gregory, K.S., Acharya, K.R., Liu, S.M. Description: Botulinum neurotoxin A5 cell binding domain in complex with GM1b olig... |
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The | ==Botulinum neurotoxin A5 cell binding domain in complex with GM1b oligosaccharide== | ||
<StructureSection load='7qpu' size='340' side='right'caption='[[7qpu]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7qpu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C1IPK2_CLOBO C1IPK2_CLOBO] | |||
<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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7qpu" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Liu | ==See Also== | ||
*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Clostridium botulinum]] | |||
[[Category: Large Structures]] | |||
[[Category: Acharya KR]] | |||
[[Category: Gregory KS]] | |||
[[Category: Liu SM]] | |||
Latest revision as of 16:20, 1 February 2024
Botulinum neurotoxin A5 cell binding domain in complex with GM1b oligosaccharideBotulinum neurotoxin A5 cell binding domain in complex with GM1b oligosaccharide
Structural highlights
FunctionPublication Abstract from PubMedBotulinum 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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