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dc.contributorWichita State University. Department of Chemistryen_US
dc.contributor.authorRajapaksha, Maheshinieen_US
dc.contributor.authorEichler, Jack F.en_US
dc.contributor.authorHajduch, Janen_US
dc.contributor.authorAnderson, David E.en_US
dc.contributor.authorKirk, Kenneth L.en_US
dc.contributor.authorBann, James G.en_US
dc.date.accessioned2012-02-06T17:16:06Z
dc.date.available2012-02-06T17:16:06Z
dc.date.issued2009-01-01en_US
dc.identifier19177347en_US
dc.identifier9211750en_US
dc.identifierUS4 AJ1057160en_US
dc.identifier.citationProtein science : a publication of the Protein Society. 2009 Jan; 18(1): 17-23.en_US
dc.identifier.issn1469-896Xen_US
dc.identifier.issn0961-8368en_US
dc.identifier.urihttp://dx.doi.org/10.1002/pro.26en_US
dc.identifier.urihttp://hdl.handle.net/10057/4308
dc.descriptionClick on the DOI link below to access the article.en_US
dc.description.abstractThe 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.sponsorshipPHS HHSen_US
dc.format.extent17-23en_US
dc.language.isoengen_US
dc.publisherJohn Wiley and Sonsen_US
dc.relation.ispartofseriesProtein science : a publication of the Protein Societyen_US
dc.relation.ispartofseriesProtein Sci.en_US
dc.sourceNLMen_US
dc.subjectResearch Support, N.I.H., Extramuralen_US
dc.subjectResearch Support, Non-U.S. Gov'ten_US
dc.subject.meshAntigens, Bacterial/chemistryen_US
dc.subject.meshBacillus anthracis/metabolism*en_US
dc.subject.meshBacterial Toxins/chemistryen_US
dc.subject.meshCarbon Isotopes/metabolismen_US
dc.subject.meshCell Membrane/metabolismen_US
dc.subject.meshHistidine/metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshMembrane Proteins/chemistryen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_US
dc.subject.meshProtein Binding/physiologyen_US
dc.subject.meshvon Willebrand Factor/metabolismen_US
dc.subject.meshAntigens, Bacterial/metabolismen_US
dc.subject.meshBacterial Toxins/metabolismen_US
dc.subject.meshMembrane Proteins/metabolismen_US
dc.titleMonitoring anthrax toxin receptor dissociation from the protective antigen by NMRen_US
dc.typeArticleen_US
dc.coverage.spacialUnited Statesen_US
dc.description.versionPeer revieweden_US
dc.rights.holderCopyright © 2008 The Protein Societyen_US


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