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2021 ; 39
(11
): 4015-4025
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Structural and simulation analysis of hotspot residues interactions of SARS-CoV 2
with human ACE2 receptor
#MMPMID32448098
J Biomol Struct Dyn
2021[Jul]; 39
(11
): 4015-4025
PMID32448098
show ga
The novel corona virus disease 2019 (SARS-CoV 2) pandemic outbreak was alarming.
The binding of SARS-CoV (CoV) spike protein (S-Protein) Receptor Binding Domain
(RBD) to Angiotensin converting enzyme 2 (ACE2) receptor initiates the entry of
corona virus into the host cells leading to the infection. However, considering
the mutations reported in the SARS-CoV 2 (nCoV), the structural changes and the
binding interactions of the S-protein RBD of nCoV were not clear. The present
study was designed to elucidate the structural changes, hot spot binding residues
and their interactions between the nCoV S-protein RBD and ACE2 receptor through
computational approaches. Based on the sequence alignment, a total of 58 residues
were found mutated in nCoV S-protein RBD. These mutations led to the structural
changes in the nCoV S-protein RBD 3d structure with 4 helices, 10 sheets and
intermittent loops. The nCoV RBD was found binding to ACE2 receptor with 11
hydrogen bonds and 1 salt bridge. The major hot spot amino acids involved in the
binding identified by interaction analysis after simulations includes Glu 35, Tyr
83, Asp 38, Lys 31, Glu 37, His 34 amino acid residues of ACE2 receptor and Gln
493, Gln 498, Asn 487, Tyr 505 and Lys 417 residues in nCoV S-protein RBD. Based
on the hydrogen bonding, RMSD and RMSF, total and potential energies, the nCoV
was found binding to ACE2 receptor with higher stability and rigidity.
Concluding, the hotspots information will be useful in designing blockers for the
nCoV spike protein RBD. [Formula: see text]Communicated by Ramaswamy H. Sarma.