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4isq

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Revision as of 22:40, 25 December 2014

Binding domain of Botulinum neurotoxin DC in complex with human synaptotagmin I

Structural highlights

4isq is a 6 chain structure with sequence from Clostridium botulinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4isr
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Berntsson RP, Peng L, Svensson LM, Dong M, Stenmark P. Crystal Structures of Botulinum Neurotoxin DC in Complex with Its Protein Receptors Synaptotagmin I and II. Structure. 2013 Sep 3;21(9):1602-11. doi: 10.1016/j.str.2013.06.026. Epub 2013, Aug 8. PMID:23932591 doi:http://dx.doi.org/10.1016/j.str.2013.06.026

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4isq"

@@ Line 7: / Line 7: @@
 <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://www.rcsb.org/pdb/explore.do?structureId=4isq RCSB], [http://www.ebi.ac.uk/pdbsum/4isq PDBsum]</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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4isq

From Proteopedia

Revision as of 22:40, 25 December 2014

Binding domain of Botulinum neurotoxin DC in complex with human synaptotagmin I

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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