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4qd2

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Revision as of 08:50, 4 August 2016

Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex

Structural highlights

4qd2 is a 10 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CADH1_MOUSE] Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity). E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production (By similarity).

Publication Abstract from PubMed

How botulinum neurotoxins (BoNTs) cross the host intestinal epithelial barrier in foodborne botulism is poorly understood. Here, we present the crystal structure of a clostridial hemagglutinin (HA) complex of serotype BoNT/A bound to the cell adhesion protein E-cadherin at 2.4 angstroms. The HA complex recognizes E-cadherin with high specificity involving extensive intermolecular interactions and also binds to carbohydrates on the cell surface. Binding of the HA complex sequesters E-cadherin in the monomeric state, compromising the E-cadherin-mediated intercellular barrier and facilitating paracellular absorption of BoNT/A. We reconstituted the complete 14-subunit BoNT/A complex using recombinantly produced components and demonstrated that abolishing either E-cadherin- or carbohydrate-binding of the HA complex drastically reduces oral toxicity of BoNT/A complex in vivo. Together, these studies establish the molecular mechanism of how HAs contribute to the oral toxicity of BoNT/A.

Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex.,Lee K, Zhong X, Gu S, Kruel AM, Dorner MB, Perry K, Rummel A, Dong M, Jin R Science. 2014 Jun 20;344(6190):1405-10. doi: 10.1126/science.1253823. PMID:24948737^[1]

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

References

↑ Lee K, Zhong X, Gu S, Kruel AM, Dorner MB, Perry K, Rummel A, Dong M, Jin R. Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex. Science. 2014 Jun 20;344(6190):1405-10. doi: 10.1126/science.1253823. PMID:24948737 doi:http://dx.doi.org/10.1126/science.1253823

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4qd2"

@@ Line 1: / Line 1: @@
 ==Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex==
 <StructureSection load='4qd2' size='340' side='right' caption='[[4qd2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4qd2]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QD2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QD2 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=4qd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qd2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qd2 RCSB], [http://www.ebi.ac.uk/pdbsum/4qd2 PDBsum]</span></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=4qd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qd2 OCA], [http://pdbe.org/4qd2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qd2 RCSB], [http://www.ebi.ac.uk/pdbsum/4qd2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qd2 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4qd2" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cadherin|Cadherin]]
+*[[Hemagglutinin|Hemagglutinin]]
 == References ==
 <references/>

4qd2

From Proteopedia

Revision as of 08:50, 4 August 2016

Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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