Structural highlights
Publication Abstract from PubMed
The exact residues within severe acute respiratory syndrome coronavirus (SARS-CoV) S1 protein and its receptor, human ACE2, involved in their interaction still remain largely undetermined. Identification of exact amino acid residues that are crucial for the interaction of S1 with ACE2 could provide working hypotheses for experimental studies and might be helpful for the development of antiviral inhibitor. In this paper, a molecular docking model of SARS-CoV S1 protein in complex with human ACE2 was constructed. The interacting residue pairs within this complex model and their contact types were also identified. Our model, supported by significant biochemical evidence, suggested receptor-binding residues were concentrated in two segments of S1 protein. In contrast, the interfacial residues in ACE2, though close to each other in tertiary structure, were found to be widely scattered in the primary sequence. In particular, the S1 residue ARG453 and ACE2 residue LYS341 might be the key residues in the complex formation.
A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2.,Zhang Y, Zheng N, Hao P, Cao Y, Zhong Y Comput Biol Chem. 2005 Jun;29(3):254-7. PMID:15979045[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang Y, Zheng N, Hao P, Cao Y, Zhong Y. A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2. Comput Biol Chem. 2005 Jun;29(3):254-7. PMID:15979045 doi:10.1016/j.compbiolchem.2005.04.008
