View source for Structural and functional analysis of the Nipah virus polymerase complex

'''Authors:''' Side Hu, Heesu Kim, Pan Yang, Zishuo Yu, Barbara Ludeke, Shawna Mobilia, Junhua Pan, Margaret Stratton, Yuemin Bian, Rachel Fearns, Jonathan Abraham

'''Year:''' 2025

'''Journal:''' Cell

'''DOI:''' 10.1016/j.cell.2024.12.021

=== Summary ===
The paper determines the cryoelectron microscopy (cryo-EM) structure of the Nipah virus polymerase complex and performs structural, biophysical, and functional analyses to understand features critical for RNA replication and transcription. The findings could aid in the development of antivirals.

=== Key Findings ===
* Cryo-EM structure of the NiV L-P complex determined
* Docking studies with an inhibitor clarify mechanisms of intrinsic NiV L resistance
* Palm insert, zinc fingers, and P4 extension are critical for NiV L activity
* Intrusion loop plays an essential role in RNA replication

=== Methodology ===
* '''Study Type:''' Structural analysis/Functional analysis

=== Topics ===
Virology, Pharmacology

=== Relevance ===
The paper's findings have implications for understanding Nipah virus replication and developing antivirals.

=== Source ===
View the entire paper: [[File:main (2).pdf]]