Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural modeling of Omicron spike protein and its complex with human ACE-2 receptor: Molecular basis for high transmissibility of the virus.

Biochemical and biophysical research communications - 12 Feb 2022

Koley Tirthankar, Kumar Manoj, Goswami Arunima, Ethayathulla Abdul S, Hariprasad Gururao

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Angiotensin-Converting Enzyme 2
Share to Biophysical Phenomena

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Host Microbial Interactions

Share to Molecular Dynamics Simulation

Share to Pandemics

Share to Protein Interaction Domains and Motifs

Share to Spike Glycoprotein, Coronavirus

Share to Structural Homology, Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 35026605
DOI: 10.1016/j.bbrc.2021.12.082
PMCID: PMC8739823

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural modeling of Omicron spike protein and its complex with human ACE-2 receptor: Molecular basis for high transmissibility of the virus.PMID 35026605Read ↗

Improved binding affinity of the Omicron’s spike protein with hACE2 receptor is the key factor behind its increased virulenceSemantic proximity Read ↗

Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2.Semantic proximity Read ↗

A Computational Dissection of Spike protein of SARS-CoV-2 Omicron VariantSemantic proximity Read ↗

Analyzing the interaction of human ACE2 and RBD of spike protein of SARS-CoV-2 in perspective of Omicron variantSemantic proximity Read ↗

Omicron Spike Protein Has a Positive Electrostatic Surface That Promotes ACE2 Recognition and Antibody EscapeSemantic proximity Read ↗

Mutations in the Receptor Binding Domain of Severe Acute Respiratory Coronavirus-2 Omicron Variant Spike Protein Significantly Stabilizes Its Conformation.Semantic proximity Read ↗

Mutations on RBD of SARS-CoV-2 Omicron variant result in stronger binding to human ACE2 receptorSemantic proximity Read ↗

Assessment of Mutations on RBD in the Spike Protein of SARS-CoV-2 Alpha, Delta and Omicron VariantsSemantic proximity Read ↗

Omicron Spike protein has a positive electrostatic surface that promotes ACE2 recognition and antibody escapeSemantic proximity Read ↗

Mutations on RBD of SARS-CoV-2 Omicron variant result in stronger binding to human ACE2 receptor.Semantic proximity Read ↗

Deciphering the Impact of Mutations on the Binding Efficacy of SARS-CoV-2 Omicron and Delta Variants With Human ACE2 ReceptorSemantic proximity Read ↗

Insights into the structural peculiarities of the N-terminal and receptor binding domains of the spike protein from the SARS-CoV-2 Omicron variant.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.