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Protein Complexes with Interchangeable Parts01:57

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Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Related Experiment Video

Updated: Oct 12, 2025

Author Spotlight: Functional Site-Directed Fluorometry in Native Cells to Study Skeletal Muscle Excitability
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Structures and Functional Diversities of ASFV Proteins.

Guoguo Wang1, Mengjia Xie1, Wei Wu1

  • 1State Key Laboratory of Agrobiotechnology and Beijing Advanced Innovation Center for Food Nutrition and Human Health, College of Biological Sciences, China Agricultural University, Beijing 100193, China.

Viruses
|November 27, 2021
PubMed
Summary

African swine fever virus (ASFV) causes a deadly epidemic in swine. This study details the structures and functions of ASFV proteins, aiding in understanding and controlling this complex virus.

Keywords:
AP endonucleaseASFVAfrican swine fever virusAsfvLIGAsfvPolXdUTPasesp72pS273Rstructuressurvival

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • African swine fever virus (ASFV) is a highly contagious, double-stranded DNA virus responsible for a devastating epidemic.
  • ASFV possesses a complex structure with multiple protein layers and a large genome, contributing to its high pathogenicity and nearly 100% mortality rate in swine.
  • Despite its complexity, the structural and functional roles of most ASFV proteins remain poorly understood.

Purpose of the Study:

  • To consolidate and present all ASFV proteins with elucidated structures.
  • To explain the functions of these proteins from a structural perspective.
  • To enhance the understanding of ASFV's replication, survival, and host immune evasion mechanisms.

Main Methods:

  • Literature review and data compilation of ASFV protein structures.
  • Analysis of structural data to infer protein functions.
  • Integration of structural information with known ASFV biology.

Main Results:

  • Detailed structural information for key ASFV proteins including AP endonuclease, dUTPases (E165R), pS273R protease, core shell proteins (p15, p35), and major capsid protein p72 (B646L).
  • Structural insights into non-structural proteins (pA151R, pNP868R, A179L, pA104R, pB119L), polymerase X, and ligase.
  • Demonstration of how novel structural features and diverse protein functions contribute to ASFV's immune evasion and control challenges.

Conclusions:

  • The structural elucidation of numerous ASFV proteins provides critical insights into the virus's complex molecular mechanisms.
  • Understanding these structures is essential for developing effective strategies against ASFV.
  • The intricate structural features of ASFV facilitate its survival and pathogenesis, highlighting the need for continued research.