5tpc
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Binding domain of BoNT/A complexed with ganglioside== | |
| + | <StructureSection load='5tpc' size='340' side='right'caption='[[5tpc]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5tpc]] is a 1 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=5TPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TPC 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]] 2Å</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=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</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=5tpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tpc OCA], [https://pdbe.org/5tpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tpc RCSB], [https://www.ebi.ac.uk/pdbsum/5tpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tpc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BXA1_CLOBH BXA1_CLOBH] Inhibits acetylcholine release. The botulinum toxin binds with high affinity to peripheral neuronal presynaptic membrane to the secretory vesicle protein SV2. It binds directly to the largest luminal loop of SV2A, SV2B and SV2C. It is then internalized by receptor-mediated endocytosis. The C-terminus of the heavy chain (H) is responsible for the adherence of the toxin to the cell surface while the N-terminus mediates transport of the light chain from the endocytic vesicle to the cytosol. After translocation, the light chain (L) hydrolyzes the 197-Gln-|-Arg-198 bond in SNAP-25, thereby blocking neurotransmitter release. Inhibition of acetylcholine release results in flaccid paralysis, with frequent heart or respiratory failure. | ||
| - | + | ==See Also== | |
| - | + | *[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Berntsson | + | [[Category: Clostridium botulinum]] |
| - | [[Category: Stenmark | + | [[Category: Large Structures]] |
| - | [[Category: Svensson | + | [[Category: Berntsson RP-A]] |
| + | [[Category: Stenmark P]] | ||
| + | [[Category: Svensson LM]] | ||
Current revision
Binding domain of BoNT/A complexed with ganglioside
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