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4qd2

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'''Unreleased structure'''
 
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The entry 4qd2 is ON HOLD
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==Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex==
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<StructureSection load='4qd2' size='340' side='right'caption='[[4qd2]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4qd2]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum_A_str._Hall Clostridium botulinum A str. Hall] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QD2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qd2 OCA], [https://pdbe.org/4qd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qd2 RCSB], [https://www.ebi.ac.uk/pdbsum/4qd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qd2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A5HZZ6_CLOBH A5HZZ6_CLOBH]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Lee, K., Zhong, X., Gu, S., Kruel, A., Dorner, M.B., Perry, K., Rummel, A., Dong, M., Jin, R.
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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<ref>PMID:24948737</ref>
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Description: Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4qd2" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Cadherin 3D structures|Cadherin 3D structures]]
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*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Clostridium botulinum A str. Hall]]
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Dong M]]
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[[Category: Dorner MB]]
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[[Category: Gu S]]
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[[Category: Jin R]]
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[[Category: Kruel A]]
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[[Category: Lee K]]
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[[Category: Perry K]]
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[[Category: Rummel A]]
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[[Category: Zhong X]]

Current revision

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

PDB ID 4qd2

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