Journal
INORGANIC CHEMISTRY
Volume 61, Issue 24, Pages 8992-8996Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.inorgchem.2c01329
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Funding
- Arnold and Mabel Beckman Foundation
- National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health [R01DK019038]
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The first encoded protein of SARS-CoV-2, Nsp1, binds to the human 40S ribosome and inhibits the synthesis of host proteins, thereby suppressing the innate immune response. The last 33 residues of the unstructured C-terminus of Nsp1 adopt a specific geometric structure upon binding to the ribosome.
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.
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