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A model of the ACE2 structure and function as a SARS-CoV receptor
Ponraj Prabakaran1, Xiaodong Xiao, Dimiter S Dimitrov
1Laboratory of Experimental and Computational Biology, CCR, NCI-Frederick, NIH, Frederick, MD 21702-1201, USA.
Biochemical and Biophysical Research Communications
|January 13, 2004
Summary
Angiotensin-converting enzyme 2 (ACE2) acts as a SARS virus receptor. Structural modeling reveals a potential binding site for the SARS-CoV S-glycoprotein on ACE2, aiding future research.
Area of Science:
- Biochemistry
- Structural Biology
- Virology
Background:
- Angiotensin-converting enzyme 2 (ACE2) regulates the renin-angiotensin system.
- ACE2 is identified as a functional receptor for the SARS virus.
- ACE2 shares sequence similarity with testis-specific ACE (tACE) and Drosophila ACE (AnCE).
Purpose of the Study:
- To build a homology model of the ACE2 structure.
- To identify potential binding regions for the SARS-CoV S-glycoprotein on ACE2.
Main Methods:
- Homology modeling based on tACE and AnCE crystal structures.
- Analysis of the ACE2 structural model to identify surface features and potential binding sites.
Main Results:
- A robust homology model of ACE2 was generated with high accuracy.
- The model revealed a deep channel containing the catalytic site.
- Negatively charged ridges and hydrophobic patches on the ACE2 surface suggest a binding site for the SARS-CoV S-glycoprotein's RBD.
Conclusions:
- The study proposes a potential binding region for SARS-CoV S-glycoprotein on ACE2.
- Findings can guide further experiments to understand ACE2 structure and function in SARS infection.