Correction: Monk, B.C.; Keniya, M.V. Roles for Structural Biology in the Discovery of Drugs and Agrochemicals Targeting Sterol 14α-Demethylases. J. Fungi 2021, 7, 67
Department of Oral Sciences, Sir John Walsh Research Institute, University of Otago, Dunedin 9016, New Zealand
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Author to whom correspondence should be addressed.
J. Fungi 2021, 7(12), 1011; https://doi.org/10.3390/jof7121011
Submission received: 15 November 2021
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Accepted: 17 November 2021
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Published: 26 November 2021
(This article belongs to the Special Issue The Application of Structural Biology in Antifungal Drug Discovery)
In the original publication, there was a mistake in Figure 4. Lanosterol in the ligand-binding pocket (LBP) of CYP51 that was published [1]. The arrows retained a white instead of a transparent background and thus obscured parts of the figure. The corrected Figure 4 appears below. The authors apologize for any inconvenience caused and state that the scientific conclusions are unaffected. The original publication has also been updated.
Reference
- Monk, B.C.; Keniya, M.V. Roles for Structural Biology in the Discovery of Drugs and Agrochemicals Targeting Sterol 14α-Demethylases. J. Fungi 2021, 7, 67. [Google Scholar] [CrossRef] [PubMed]
Figure 4.
Lanosterol in the ligand-binding pocket (LBP) of CYP51. Relevant portions of the human HsCYP51 crystal structure (Protein Data Bank (PDB) 6UEZ) are shown. Residues within 4 Å of lanosterol (yellow) are shown with carbon atoms in green. These 16 residues are found in helix I, helix B, helix C, the B-C loop, the K-K’ internal loop and the C-terminal region. Proton channel S mutations, D231A in helix F and H314A in nearby helix I, are shown in white. Upon lanosterol binding helix C has changed conformation slightly, the K156 side chain loses its ionic interaction with the heme propionate C and becomes exposed into the enzyme surface. The K-K’ internal loop I379 main chain carbonyl hydrogen bonds with the OH of lanosterol. The main chain amides of M378 and I379 plus the main chain carbonyl of M487 in the C-terminal region form a water-mediated hydrogen bond network with the hydroxyl of lanosterol. The 14α-methyl group of lanosterol lies in proximity of the heme iron (large red ball) in a catalytically competent position.
Figure 4.
Lanosterol in the ligand-binding pocket (LBP) of CYP51. Relevant portions of the human HsCYP51 crystal structure (Protein Data Bank (PDB) 6UEZ) are shown. Residues within 4 Å of lanosterol (yellow) are shown with carbon atoms in green. These 16 residues are found in helix I, helix B, helix C, the B-C loop, the K-K’ internal loop and the C-terminal region. Proton channel S mutations, D231A in helix F and H314A in nearby helix I, are shown in white. Upon lanosterol binding helix C has changed conformation slightly, the K156 side chain loses its ionic interaction with the heme propionate C and becomes exposed into the enzyme surface. The K-K’ internal loop I379 main chain carbonyl hydrogen bonds with the OH of lanosterol. The main chain amides of M378 and I379 plus the main chain carbonyl of M487 in the C-terminal region form a water-mediated hydrogen bond network with the hydroxyl of lanosterol. The 14α-methyl group of lanosterol lies in proximity of the heme iron (large red ball) in a catalytically competent position.
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Monk, B.C.; Keniya, M.V. Correction: Monk, B.C.; Keniya, M.V. Roles for Structural Biology in the Discovery of Drugs and Agrochemicals Targeting Sterol 14α-Demethylases. J. Fungi 2021, 7, 67. J. Fungi 2021, 7, 1011. https://doi.org/10.3390/jof7121011
AMA Style
Monk BC, Keniya MV. Correction: Monk, B.C.; Keniya, M.V. Roles for Structural Biology in the Discovery of Drugs and Agrochemicals Targeting Sterol 14α-Demethylases. J. Fungi 2021, 7, 67. Journal of Fungi. 2021; 7(12):1011. https://doi.org/10.3390/jof7121011
Chicago/Turabian StyleMonk, Brian C., and Mikhail V. Keniya. 2021. "Correction: Monk, B.C.; Keniya, M.V. Roles for Structural Biology in the Discovery of Drugs and Agrochemicals Targeting Sterol 14α-Demethylases. J. Fungi 2021, 7, 67" Journal of Fungi 7, no. 12: 1011. https://doi.org/10.3390/jof7121011
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