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 |