Morales, Maryann and Ravanfar, Raheleh and Oyala, Paul H. and Gray, Harry B. and Winkler, Jay R. (2022) Copper(II) Binding to the Intrinsically Disordered C-Terminal Peptide of SARS-CoV-2 Virulence Factor Nsp1. Inorganic Chemistry, 61 (24). pp. 8992-8996. ISSN 0020-1669. PMCID PMC9195567. doi:10.1021/acs.inorgchem.2c01329. https://resolver.caltech.edu/CaltechAUTHORS:20220606-736150000
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Abstract
The first encoded SARS-CoV-2 protein (Nsp1) binds to the human 40S ribosome and blocks synthesis of host proteins, thereby inhibiting critical elements of the innate immune response. The final 33 residues of the natively unstructured Nsp1 C-terminus adopt a helix-turn-helix geometry upon binding to the ribosome. We have characterized the fluctuating conformations of this peptide using circular dichroism spectroscopy along with measurements of tryptophan fluorescence and energy transfer. Tryptophan fluorescence decay kinetics reveal that copper(II) binds to the peptide at micromolar concentrations, and electron paramagnetic resonance spectroscopy indicates that the metal ion coordinates to the lone histidine residue.
| Item Type: | Article | ||||||||||||
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| Additional Information: | © 2022 American Chemical Society. This article is made available via the ACS COVID-19 subset for unrestricted RESEARCH re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. Received: April 19, 2022; Published: June 6, 2022. The work was supported by the Arnold and Mabel Beckman Foundation and by the National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health under Award R01DK019038. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. The authors declare no competing financial interest. | ||||||||||||
| Group: | COVID-19 | ||||||||||||
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| Subject Keywords: | Chemical structure, Electron paramagnetic resonance spectroscopy, Fluorescence, Peptides and proteins, SARS-CoV-2 | ||||||||||||
| Issue or Number: | 24 | ||||||||||||
| PubMed Central ID: | PMC9195567 | ||||||||||||
| DOI: | 10.1021/acs.inorgchem.2c01329 | ||||||||||||
| Record Number: | CaltechAUTHORS:20220606-736150000 | ||||||||||||
| Persistent URL: | https://resolver.caltech.edu/CaltechAUTHORS:20220606-736150000 | ||||||||||||
| Official Citation: | Copper(II) Binding to the Intrinsically Disordered C-Terminal Peptide of SARS-CoV-2 Virulence Factor Nsp1. Maryann Morales, Raheleh Ravanfar, Paul H. Oyala, Harry B. Gray, and Jay R. Winkler. Inorganic Chemistry 2022 61 (24), 8992-8996; DOI: 10.1021/acs.inorgchem.2c01329 | ||||||||||||
| Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. | ||||||||||||
| ID Code: | 115031 | ||||||||||||
| Collection: | CaltechAUTHORS | ||||||||||||
| Deposited By: | George Porter | ||||||||||||
| Deposited On: | 07 Jun 2022 15:48 | ||||||||||||
| Last Modified: | 28 Jun 2022 19:39 |
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