Receptor and viral determinants of SARS‐coronavirus adaptation to human ACE2
Introduction
Results
Localization of the S‐protein‐binding domain on human ACE2
S‐protein association is independent of ACE2 conformational changes
Association of three S proteins with human and palm‐civet ACE2
S‐protein RBD determinants of association with human ACE2
kon (M−1 s−1) | koff (s−1) | Ka (M−1) | Kd (M) | |
---|---|---|---|---|
TOR2 | 7.12 × 104 | 1.16 × 10−3 | 6.20 × 107 | 1.62 × 10−8 |
K344R | 6.50 × 104 | 1.04 × 10−3 | 6.27 × 107 | 1.60 × 10−8 |
F360S | 6.23 × 104 | 8.80 × 10−4 | 7.08 × 107 | 1.41 × 10−8 |
N479K | 5.73 × 104 | 2.77 × 10−2 | 2.07 × 106 | 4.84 × 10−7 |
T487S | 3.88 × 104 | 1.37 × 10−2 | 2.84 × 106 | 3.52 × 10−7 |
SZ3 | 42.6 | 2.35 × 10−2 | 1.81 × 103 | 5.51 × 10−4 |
Palm‐civet and human ACE2 determinants of differential S‐protein association
Binding of RBD chimeras to ACE2 chimeras
Mapping determinants to the ACE2 surface
Discussion
Materials and methods
Construction of S‐protein and ACE2 variants
Binding assays
Infection with S‐protein‐pseudotyped retrovirus
ACE2 enzymatic activity
Supplementary data
Supporting Information
References
Information & Authors
Information
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Butterfly in motion - Captured at the Museum of Life and Sciences, Durham USA, with a Canon EOS 300D, EF 75-300 mm f/4.0-5.6 USM lens. The photographer, Nikolay V. Dokholyan, is an Assistant Professor at the Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, USA. Dokholyan's group focuses primarily on understanding protein dynamics and on how induced changes in protein folding lead to disease.
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