1st International and 10th National Iranian Conference on Bioinformatics
Home Accepted Papers
Comparative molecular dynamics study of receptor-binding domains in wild type and Omicron (B.1.1.529) variant of SARS-CoV-2
Paper ID : 1184-ICB10
Authors:
Negin Safaei Hashkavaei1, Fatemeh Bayani2, Yahya Sefidbakht *3
1مرکز تحقیقات پروتئین- دانشگاه شهیدبهشتی- تهران- ایران
2مرکز تحقیقات پروتئین- دانشگاه شهید بهشتی- تهران -ایران
3مرکز تحقیقات پروتئین- دانشگاه شهیدبهشتی-تهران-ایران
Abstract:
The new variant of SARS-CoV-2, Omicron (B.1.1.529), first reported in November 2021 is currently infecting people around the world. Since the spike glycoprotein plays a key role in the early events in viral replication through a receptor binding domain (RBD) which bindes to angiotensin-converting enzyme 2 (ACE2), it is important to study the effects of mutations on the structure of receptor binding domain (RBD) [1]. Based on Structural analysis, 15 substitution mutations were identified in RBD of this new variant. In this paper, we used computational comparison of receptor-binding domain (RBD) in wild-type (WT) SARS-CoV-2 and Omicron variant of concern (VOC) in free forms and structural models were built using the I-TASSER server. Based on our molecular dynamics simulation results, mutations can affect the RBD structure and in this new variant of concern, RBD structure is more open than the wild-type (WT) RBD. The results of this study could help to achieve a better understanding for researchers, and be effective in the development of novel therapies.
Keywords:
Receptor-binding domain (RBD); SARS-CoV-2; Omicron (B.1.1.529); Molecular dynamics simulations.
Status : Paper Accepted (Poster Presentation)