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Monitoring anthrax toxin receptor dissociation from the protective antigen by NMR

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dc.contributor Wichita State University. Department of Chemistry en_US
dc.contributor.author Rajapaksha, Maheshinie en_US
dc.contributor.author Eichler, Jack F. en_US
dc.contributor.author Hajduch, Jan en_US
dc.contributor.author Anderson, David E. en_US
dc.contributor.author Kirk, Kenneth L. en_US
dc.contributor.author Bann, James G. en_US
dc.date.accessioned 2012-02-06T17:16:06Z
dc.date.available 2012-02-06T17:16:06Z
dc.date.issued 2009-01-01 en_US
dc.identifier 19177347 en_US
dc.identifier 9211750 en_US
dc.identifier US4 AJ1057160 en_US
dc.identifier.citation Protein science : a publication of the Protein Society. 2009 Jan; 18(1): 17-23. en_US
dc.identifier.issn 1469-896X en_US
dc.identifier.issn 0961-8368 en_US
dc.identifier.uri http://dx.doi.org/10.1002/pro.26 en_US
dc.identifier.uri http://hdl.handle.net/10057/4308
dc.description Click on the DOI link below to access the article. en_US
dc.description.abstract The binding of the Bacillus anthracis protective antigen (PA) to the host cell receptor is the first step toward the formation of the anthrax toxin, a tripartite set of proteins that include the enzymatic moieties edema factor (EF), and lethal factor (LF). PA is cleaved by a furin-like protease on the cell surface followed by the formation of a donut-shaped heptameric prepore. The prepore undergoes a major structural transition at acidic pH that results in the formation of a membrane spanning pore, an event which is dictated by interactions with the receptor and necessary for entry of EF and LF into the cell. We provide direct evidence using 1-dimensional (13)C-edited (1)H NMR that low pH induces dissociation of the Von-Willebrand factor A domain of the receptor capillary morphogenesis protein 2 (CMG2) from the prepore, but not the monomeric full length PA. Receptor dissociation is also observed using a carbon-13 labeled, 2-fluorohistidine labeled CMG2, consistent with studies showing that protonation of His-121 in CMG2 is not a mechanism for receptor release. Dissociation is likely caused by the structural transition upon formation of a pore from the prepore state rather than protonation of residues at the receptor PA or prepore interface. en_US
dc.description.sponsorship PHS HHS en_US
dc.format.extent 17-23 en_US
dc.language.iso eng en_US
dc.publisher John Wiley and Sons en_US
dc.relation.ispartofseries Protein science : a publication of the Protein Society en_US
dc.relation.ispartofseries Protein Sci. en_US
dc.source NLM en_US
dc.subject Research Support, N.I.H., Extramural en_US
dc.subject Research Support, Non-U.S. Gov't en_US
dc.subject.mesh Antigens, Bacterial/chemistry en_US
dc.subject.mesh Bacillus anthracis/metabolism* en_US
dc.subject.mesh Bacterial Toxins/chemistry en_US
dc.subject.mesh Carbon Isotopes/metabolism en_US
dc.subject.mesh Cell Membrane/metabolism en_US
dc.subject.mesh Histidine/metabolism en_US
dc.subject.mesh Humans en_US
dc.subject.mesh Hydrogen-Ion Concentration en_US
dc.subject.mesh Membrane Proteins/chemistry en_US
dc.subject.mesh Models, Molecular en_US
dc.subject.mesh Nuclear Magnetic Resonance, Biomolecular en_US
dc.subject.mesh Protein Binding/physiology en_US
dc.subject.mesh von Willebrand Factor/metabolism en_US
dc.subject.mesh Antigens, Bacterial/metabolism en_US
dc.subject.mesh Bacterial Toxins/metabolism en_US
dc.subject.mesh Membrane Proteins/metabolism en_US
dc.title Monitoring anthrax toxin receptor dissociation from the protective antigen by NMR en_US
dc.type Article en_US
dc.coverage.spacial United States en_US
dc.description.version Peer reviewed en_US
dc.rights.holder Copyright © 2008 The Protein Society en_US

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