@article{9150123a9d4d434482c57e9655ef5956,
title = "Crystal structure and transient dimerization for the FKBP12 protein from the pathogenic fungus Candida auris",
abstract = "International concern over the recent emergence of Candida auris infections reflects not only its comparative ease of transmission and substantial mortality but the increasing level of resistance observed to all three major classes of antifungal drugs. Diminution in virulence has been reported for a wide range of fungal pathogens when the FK506-binding protein FKBP12 binds to that immunosuppressant drug and the binary complex then inhibits the fungal calcineurin signaling pathway. Structure-based drug design efforts have described modifications of FK506 which modestly reduce virulence for a number of fungal pathogens while also lessening the side effect of suppressing the tissue immunity response in the patient. To aid in such studies, we report the crystal structure of Candida auris FKBP12. As physiological relevance has been proposed for transient homodimerization interactions of distantly related fungal FKBP12 proteins, we report the solution NMR characterization of the homodimerization interactions of the FKBP12 proteins from both Candida auris and Candida glabrata.",
keywords = "Candida auris, Candida glabrata, Chemical shift perturbation, Crystal structure, FKBP12, Multi-drug resistance",
author = "Qamar Bashir and Zhong Li and Hongmin Li and LeMaster, {David M.} and Griselda Hern{\'a}ndez",
note = "Funding Information: We thank Dr. Kevin Battaile at the National Synchrotron Light Source II (NSLS II) for help in data collection and processing. Use of the NYX beamline 19-ID at NSLS II was supported by the member institutions of the New York Structural Biology Center. This research used resources of the National Synchrotron Light Source II, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Brookhaven National Laboratory under Contract No. DE-SC0012704 . We also acknowledge the use of the NMR core facility at the Wadsworth Center . Grant support for this research was provided by National Institutes of Health GM 119152 [G.H.]. Molecular graphics performed with UCSF Chimera, developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco , with support from NIH P41-GM103311 . Funding Information: We thank Dr. Kevin Battaile at the National Synchrotron Light Source II (NSLS II) for help in data collection and processing. Use of the NYX beamline 19-ID at NSLS II was supported by the member institutions of the New York Structural Biology Center. This research used resources of the National Synchrotron Light Source II, a U.S. Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by Brookhaven National Laboratory under Contract No. DE-SC0012704. We also acknowledge the use of the NMR core facility at the Wadsworth Center. Grant support for this research was provided by National Institutes of Health GM 119152 [G.H.]. Molecular graphics performed with UCSF Chimera, developed by the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco, with support from NIH P41-GM103311. Publisher Copyright: {\textcopyright} 2020 Wadsworth Center, New York State Department of Health",
year = "2020",
month = may,
day = "14",
doi = "10.1016/j.bbrc.2020.03.059",
language = "English (US)",
volume = "525",
pages = "1103--1108",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "4",
}