Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

The Binding Mechanism of Coronavirus Disease 2019 with Human Angiotensin Converting Enzyme 2

Version 1 : Received: 9 May 2020 / Approved: 11 May 2020 / Online: 11 May 2020 (04:08:26 CEST)

How to cite: Lone, B.; Lone, M. The Binding Mechanism of Coronavirus Disease 2019 with Human Angiotensin Converting Enzyme 2. Preprints 2020, 2020050186. https://doi.org/10.20944/preprints202005.0186.v1 Lone, B.; Lone, M. The Binding Mechanism of Coronavirus Disease 2019 with Human Angiotensin Converting Enzyme 2. Preprints 2020, 2020050186. https://doi.org/10.20944/preprints202005.0186.v1

Abstract

The outbreak across the globe due to coronavirus disease 2019 (COVID-19) has spread abruptly by infected humans worldwide. The continuous efforts by scientists is on way to understand how pandemic of COVID-19 resembles and differs from serve acute respiratory syndrome coronavirus (SARS-CoV) at transcriptomic and genomic level. The SARS-CoV and COVID-19 exploits the angiotensin converting enzyme 2 (ACE2) receptor to gain entry inside the cells.We analyzed the entry COVID-19 into host cell due to receptor binding domain (RBD) of spike glycoprotein. The proposed simulation data shows similar ternary structures from two viruses shares approximately 80 percent identity in amino acid sequences. Our molecular modeling investigation signifies that angiotensin converting enzyme 2 (ACE2) has stronger interaction with COVID -19 RBD. The Amino acid phenylaniline F486 LOOP plays vital role due to its penetration into hydrophobic pocket in ACE2.The said investigation of S-Glycoprotein RBD of COVID-19 or SARS-CoV-2 via ACE2 provides post genome analysis of protein-protein interaction for rapid assessing transmission of infected patients by deadly CoVID-19. The scientific data extracted implies early guidance to control and viral prevention of CoVID-19.

Keywords

Coronavirus disease 2019; SARS-CoV-2; ACE2; RBD; Molecular modelling

Subject

Biology and Life Sciences, Anatomy and Physiology

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