Crucial Role of H322 in Folding of the Diphtheria Toxin T-Domain into the Open-Channel State
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, Kansas 66160, United States
2. Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi400249f
Reference25 articles.
1. Mechanism of Diphtheria Toxin Catalytic Domain Delivery to the Eukaryotic Cell Cytosol and the Cellular Factors that Directly Participate in the Process
2. Refined structure of monomelic diphtheria toxin at 2.3 Å resolution
3. Conformation of the Diphtheria Toxin T Domain in Membranes: A Site-Directed Spin-Labeling Study of the TH8 Helix and TL5 Loop
4. Organization of Diphtheria Toxin T Domain in Bilayers: A Site-Directed Spin Labeling Study
5. Topography of Diphtheria Toxin's T Domain in the Open Channel State
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