ArticleBiochemical and biophysical research communications2022
Structural modeling of Omicron spike protein and its complex with human ACE-2 receptor: Molecular basis for high transmissibility of the virus.
Article in Biochemical and biophysical research communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 33 citations in OpenAlex.
- Molecular mechanisms of SARS-CoV-2 entry: implications for biomedical strategies.Microbiology and molecular biology reviews : MMBR · 2025Review
- Subtle Changes at the RBD/hACE2 Interface During SARS-CoV-2 Variant Evolution: A Molecular Dynamics Study.Biomolecules · 2025Article
- Computational analysis of affinity dynamics between the variants of SARS-CoV-2 spike protein (RBD) and human ACE-2 receptor.Virology journal · 2024Article
- SARS-CoV-2 Omicron Spike shows strong binding affinity and favourable interaction landscape with the TLR4/MD2 compared to other variants.Journal, genetic engineering & biotechnology · 2024Article
- Protein-protein and protein-nucleic acid binding site prediction via interpretable hierarchical geometric deep learning.GigaScience · 2024Article
- SARS-CoV-2 and Its Omicron Variants Detection with RT-RPA -CRISPR/Cas13a-Based Method at Room Temperature.Reports of biochemistry & molecular biology · 2023Article
- Development and application of an RT‒PCR assay for the identification of the delta and omicron variants of SARS-COV-2.Heliyon · 2023Article
- In silico study of SARS-CoV-2 spike protein RBD and human ACE-2 affinity dynamics across variants and Omicron subvariants.Journal of medical virology · 2023Article
- Transplantation Amid a Pandemic: The Fall and Rise of Kidney Transplantation in the United States.Transplantation direct · 2023Article
- Structural Profiles of SARS-CoV-2 Variants in India.Current microbiology · 2022Article
- Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2.Protein science : a publication of the Protein Society · 2022Article
- Emerging evidence on Omicron (B.1.1.529) SARS-CoV-2 variant.Journal of medical virology · 2022Review
- Molecular Dynamics Studies on the Structural Stability Prediction of SARS-CoV-2 Variants Including Multiple Mutants.International journal of molecular sciences · 2022Article
- Potential use of the S-protein-Angiotensin converting enzyme 2 binding pathway in the treatment of coronavirus disease 2019.Frontiers in public health · 2022Review
- Comparative Structural Analysis of Human ACE2 Receptor with Spike Protein of SARS-CoV-2 Variants: Implications to Understand Infectivity of the Virus.Advances and applications in bioinformatics and chemistry : AABC · 2022Article
- Mechanisms of Immune Dysregulation in COVID-19 Are Different From SARS and MERS: A Perspective in Context of Kawasaki Disease and MIS-C.Frontiers in pediatrics · 2022Review
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Omicron is a new variant of SARS-CoV-2, which is currently infecting people around the world. Spike glycoprotein, an important molecule in pathogenesis of infection has been modeled and the interaction of its Receptor Binding Domain with human ACE-receptor has been analysed by simulation studies. Structural analysis of Omicron spike glycoprotein shows the 30 mutations to be distributed over all domains of the trimeric protein, wherein the mutant residues are seen to be participating in higher number of intra-molecular interactions including two salt bridges emanating from mutant residues thereby stabilizing their conformation, as compared to wild type. Complex of Receptor Binding Domain (RBD) with human ACE-2 receptor shows seven mutations at interacting interface comprising of two ionic interactions, eight hydrogen bonds and seven Van der Waals interactions. The number and quality of these interactions along with other binding biophysical parameters suggests more potency of RBD domain to the receptor as compared to the wild type counterpart. Results of this study explains the high transmissibility of Omicron variant of SARS-CoV-2 that is currently observed across the world.
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