4isq: Difference between revisions

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 <StructureSection load='4isq' size='340' side='right'caption='[[4isq]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4isq]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ISQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ISQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4isq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ISQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ISQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4isr|4isr]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4isq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4isq OCA], [http://pdbe.org/4isq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4isq RCSB], [http://www.ebi.ac.uk/pdbsum/4isq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4isq ProSAT]</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=4isq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4isq OCA], [https://pdbe.org/4isq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4isq RCSB], [https://www.ebi.ac.uk/pdbsum/4isq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4isq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SYT1_HUMAN SYT1_HUMAN]] May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
+[https://www.uniprot.org/uniprot/Q9LBR1_CLOBO Q9LBR1_CLOBO]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Botulinum neurotoxins (BoNTs) can cause paralysis at exceptionally low concentrations and include seven serotypes (BoNT/A-G). The chimeric BoNT/DC toxin has a receptor binding domain similar to the same region in BoNT/C. However, BoNT/DC does not share protein receptor with BoNT/C. Instead, it shares synaptotagmin (Syt) I and II as receptors with BoNT/B, despite their low sequence similarity. Here, we present the crystal structures of the binding domain of BoNT/DC in complex with the recognition domains of its protein receptors, Syt-I and Syt-II. The structures reveal that BoNT/DC possesses a Syt binding site, distinct from the established Syt-II binding site in BoNT/B. Structure-based mutagenesis further shows that hydrophobic interactions play a key role in Syt binding. The structures suggest that the BoNT/DC ganglioside binding sites are independent of the protein receptor binding site. Our results reveal the remarkable versatility in the receptor recognition of the BoNTs.
-Crystal Structures of Botulinum Neurotoxin DC in Complex with Its Protein Receptors Synaptotagmin I and II.,Berntsson RP, Peng L, Svensson LM, Dong M, Stenmark P Structure. 2013 Sep 3;21(9):1602-11. doi: 10.1016/j.str.2013.06.026. Epub 2013, Aug 8. PMID:23932591<ref>PMID:23932591</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4isq" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
 *[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus botulinus van ermengem 1896]]
+[[Category: Clostridium botulinum]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Berntsson, R P.A]]
+[[Category: Berntsson RP-A]]
-[[Category: Dong, M]]
+[[Category: Dong M]]
-[[Category: Peng, L]]
+[[Category: Peng L]]
-[[Category: Stenmark, P]]
+[[Category: Stenmark P]]
-[[Category: Svensson, L M]]
+[[Category: Svensson LM]]
-[[Category: Membrane binding]]
-[[Category: Synaptotagmin and ganglioside binding]]
-[[Category: Toxin]]