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The complex structure of GRL0617 and SARS-CoV-2 PLpro reveals a hot spot for antiviral drug discovery

Medicine and Health

The complex structure of GRL0617 and SARS-CoV-2 PLpro reveals a hot spot for antiviral drug discovery

Z. Fu, B. Huang, et al.

This groundbreaking research by Ziyang Fu and colleagues reveals GRL0617 as a potent inhibitor of SARS-CoV-2 papain-like protease (PLpro), shedding light on its structural interactions and potential for antiviral drug development.

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Playback language: English
Abstract
SARS-CoV-2 papain-like protease (PLpro) plays crucial roles in viral maturation and immune response dysregulation, making it a promising drug target. This study screened a drug library, identifying GRL0617 as a potent PLpro inhibitor. The co-crystal structure of SARS-CoV-2 PLpro with GRL0617 reveals a non-covalent interaction within the USP domain. NMR data demonstrates GRL0617 blocks ISG15 C-terminus binding to PLpro, highlighting this pocket as a crucial hot spot for antiviral drug development.
Publisher
Nature Communications
Published On
Jan 20, 2021
Authors
Ziyang Fu, Bin Huang, Jinle Tang, Shuyan Liu, Ming Liu, Yuxin Ye, Zhihong Liu, Yuxian Xiong, Wenning Zhu, Dan Cao, Jihui Li, Xiaogang Niu, Huan Zhou, Yong Juan Zhao, Guoliang Zhang, Hao Huang
Tags
SARS-CoV-2
PLpro inhibitor
GRL0617
antiviral drug
structural biology
NMR
immune response

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