| 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 |