Structure analysis of the receptor binding of 2019-nCoV
By Yun Chen, Yao Guo, Yihang Pan, Z. Zhao. Biochemical and Biophysical Research Communications - BBRC, 2020
752 citations recorded by the source corpus.
2019-nCoV is a newly identified coronavirus with high similarity to SARS-CoV. We performed a structural analysis of the receptor binding domain (RBD) of spike glycoprotein responsible for entry of coronaviruses into host cells. The RBDs from the two viruses share 72% identity in amino acid sequences, and molecular simulation reveals highly similar ternary structures. However, 2019-nCoV has a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV. Molecular modeling revealed that 2019-nCoV RBD has a stronger interaction with angiotensin converting enzyme 2 (ACE2). A unique phenylalanine F486 in the flexible loop likely plays a major role because its penetration into a deep hydrophobic pocket in ACE2. ACE2 is widely expressed with conserved primary structures throughout the animal kingdom from fish, amphibians, reptiles, birds, to mammals. Structural analysis suggests that ACE2 from these animals can potentially bind RBD of 2019-nCoV, making them all possible natural hosts for the virus. 2019-nCoV is thought to be transmitted through respiratory droplets. However, since ACE2 is predominantly expressed in intestines, testis, and kidney, fecal-oral and other routes of transmission are also possible. Finally, antibodies and small molecular inhibitors that can block the interaction of ACE2 with RBD should be developed to combat the virus.
Subfields: Animal Science and Zoology, Infectious Diseases
View Paper: https://www.semanticscholar.org/paper/c1bc598ecb7e221eee2b84885efcf770dc12245e
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Citations in the corpus
- Angiotensin receptor blockers as tentative SARS‐CoV‐2 therapeutics (2020, positive): “However, SARS-CoV-2 includes a distinct loop with flexible glycyl residues replacing rigid prolyl residues in SARS-CoV, and molecular modeling indicated that the receptor binding domain of SARS-CoV-2 has higher affinity for ACE2 compared with SARS-CoV (Chen et al., 2020).”
- Structural and functional properties of SARS-CoV-2 spike protein: potential antivirus drug development for COVID-19 (2020, background): “Interaction between the S protein and ACE2 can be used to identify intermediate hosts of SARS-CoV-2, as ACE2 from different species, such as amphibians, birds, and mammals, has a conserved primary structure [38].”