A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2
- 30 June 2005
- journal article
- research article
- Published by Elsevier BV in Computational Biology and Chemistry
- Vol. 29 (3), 254-257
- https://doi.org/10.1016/j.compbiolchem.2005.04.008
Abstract
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.Keywords
This publication has 23 references indexed in Scilit:
- Structure-Based Discovery of a Novel Angiotensin-Converting Enzyme 2 InhibitorHypertension, 2004
- Retroviruses Pseudotyped with the Severe Acute Respiratory Syndrome Coronavirus Spike Protein Efficiently Infect Cells Expressing Angiotensin-Converting Enzyme 2Journal of Virology, 2004
- Cellular entry of the SARS coronavirusTrends in Microbiology, 2004
- Amino Acids 270 to 510 of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein Are Required for Interaction with ReceptorJournal of Virology, 2004
- STING Contacts: a web-based application for identification and analysis of amino acid contacts within protein structure and across protein interfacesBioinformatics, 2004
- ACE2 X-Ray Structures Reveal a Large Hinge-bending Motion Important for Inhibitor Binding and CatalysisPublished by Elsevier BV ,2004
- A 193-Amino Acid Fragment of the SARS Coronavirus S Protein Efficiently Binds Angiotensin-converting Enzyme 2Published by Elsevier BV ,2004
- Reconstruction of the most recent common ancestor sequences of SARS-Cov S gene and detection of adaptive evolution in the spike proteinChinese Science Bulletin, 2004
- Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirusNature, 2003
- The Protein Data BankNucleic Acids Research, 2000