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Related Experiment Video

Updated: Feb 14, 2026

Author Spotlight: Advancements in Multiplex Detection of Respiratory Viruses

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Published on: November 10, 2023

Structural Basis and Inhibitor Development of SARS-CoV-2 Papain-like Protease.

Junshuai Wang^1,2, Yuancong Xu¹, Yishu Yang¹

¹College of Chemistry and Life Science, Beijing University of Technology, Beijing 100124, China.

Molecules (Basel, Switzerland)

|February 13, 2026

Summary

Papain-like protease (PLpro) is vital for SARS-CoV-2 replication and immune evasion. Analyzing over 100 structures reveals key binding sites for developing novel antiviral inhibitors targeting PLpro.

Keywords:

SARS-CoV-2 crystal structure drug discovery papain-like protease

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Pharmacophore Modeling for Targets with Extensive Ligand Libraries: A Case Study on SARS-CoV-2 Mpro

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Pharmacophore Modeling for Targets with Extensive Ligand Libraries: A Case Study on SARS-CoV-2 Mpro

Pharmacophore Modeling for Targets with Extensive Ligand Libraries: A Case Study on SARS-CoV-2 Mpro

Published on: September 26, 2025

Area of Science:

Virology
Structural Biology
Drug Discovery

Background:

Papain-like protease (PLpro) is essential for SARS-CoV-2 replication.
PLpro, part of nsp3, hydrolyzes viral proteins and modulates host immunity.
Its critical roles make PLpro a prime target for antiviral drug development.

Purpose of the Study:

To review and analyze PLpro-ligand co-crystal structures.
To summarize major ligand binding modes to PLpro.
To inform future structure-guided design of PLpro inhibitors.

Main Methods:

Analysis of over 100 PLpro-ligand co-crystal structures.
Identification and categorization of ligand binding sites.
Review of structure-activity relationships for PLpro inhibitors.

Main Results:

Most ligands bind to canonical sites (P3, P4, BL2 loop), similar to GRL0617.
Optimized inhibitors target auxiliary regions (BL2 groove, Val70 site, Cys111).
Non-canonical/allosteric sites (S1, S2, zinc-finger) offer novel inhibitor design opportunities.

Conclusions:

Structural insights guide the optimization of PLpro inhibitors.
Targeting diverse binding sites enhances antiviral strategies.
Continued structure-guided design is crucial for effective SARS-CoV-2 therapies.