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. 2005 Jun;29(3):254-7.
doi: 10.1016/j.compbiolchem.2005.04.008.

A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2

Yuan Zhang  1 , Nan Zheng, Pei Hao, Ying Cao, Yang Zhong
Affiliations

A molecular docking model of SARS-CoV S1 protein in complex with its receptor, human ACE2

Yuan Zhang et al. Comput Biol Chem. 2005 Jun.

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.

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Figures

Fig. 1
Fig. 1
Ribbon diagram of the SARS-CoV S1 (yellow)/ACE2 (blue) complex model (PDB code: 1XJP). The theoretical model of S1 domain (PDB code: 1Q4Z) and the native crystal structure of the human ACE2 extracellular domain (PDB code: 1R42) were downloaded from the protein data bank (PDB). This model was generated by the fully automatic ZDOCK protein–protein docking server and manually selected on the basis of structural biology knowledge.
See this image and copyright information in PMC

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