P2Y12 receptor residues crucial for thrombosis regulation

Vidhya, M (2023) P2Y12 receptor residues crucial for thrombosis regulation. In: Journal of Molecular Recognition, 36 (11).

PDF jou_mol_rec_36-11_2023.pdf - Published Version Restricted to Registered users only Download (4MB) | Request a copy

Abstract

Thrombosis, or the formation of blood clots, can lead to serious medical conditions such as stroke, heart attack, and deep vein thrombosis. The purinoreceptor P2Y12 plays a critical role in the thrombotic pathway and is targeted for therapy to prevent clot formation. However, it is essential to balance the regulation of thrombosis to avoid adverse situations. This study focuses on the P2Y12 receptor and aims to discern the protein residue network and differentiate residues based on their intramolecular interactions. The study utilized a statistical analysis to characterize the significant residues involved in ligand interaction, which helps to identify critical residues that are essential for the function of the receptor. A parametric analysis of interactions of residues in the intraprotein interaction was conducted, which revealed significant residue-based contacts that facilitate protein interactions. By examining the interactions between residues, the mechanisms underlying protein interactions were studied and the importance of specific residues in facilitating these interactions was determined. This research provides important information on P2Y12, and the findings based on the network based significance of interacting residues may contribute to the development of new therapies that target the receptor to prevent clot formation while maintaining a balance in thrombosis regulation to avoid adverse outcomes. Ultimately, this study could lead to improved treatments for thrombotic disorders and better patient outcomes. © 2023 John Wiley & Sons Ltd.

Item Type:	Journal Article
Publication:	Journal of Molecular Recognition
Publisher:	John Wiley and Sons Ltd
Additional Information:	The copyright for this article belongs to the John Wiley and Sons Ltd.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	23 Nov 2023 06:47
Last Modified:	23 Nov 2023 06:47
URI:	https://eprints.iisc.ac.in/id/eprint/83216

Actions (login required)

View Item