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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Related Experiment Video

Updated: May 31, 2026

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
13:56

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions

Published on: July 18, 2013

Structural principles within the human-virus protein-protein interaction network.

Eric A Franzosa1, Yu Xia

  • 1Bioinformatics Program, Boston University, 44 Cummington Street, Boston, MA 02215, USA.

Proceedings of the National Academy of Sciences of the United States of America
|June 18, 2011
PubMed
Summary
This summary is machine-generated.

Viral proteins mimic host interactions to disrupt cell functions, revealing distinct evolutionary strategies compared to normal cell processes. This structural analysis uncovers the molecular basis of host-pathogen conflict.

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Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

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Related Experiment Videos

Last Updated: May 31, 2026

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
13:56

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions

Published on: July 18, 2013

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
10:40

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

Published on: December 21, 2019

Area of Science:

  • Structural biology
  • Systems biology
  • Evolutionary biology

Background:

  • Host-virus interactions (exogenous) are poorly understood compared to within-host interactions (endogenous).
  • Previous systems biology studies provided low-resolution host-virus interaction patterns.

Purpose of the Study:

  • To reconstruct and analyze the human-virus structural interaction network at atomic resolution.
  • To compare host-pathogen interactions with endogenous host interactions.
  • To understand the mechanistic basis and evolutionary dynamics of host-virus antagonism.

Main Methods:

  • Integrating curated and predicted 3D structural models of protein complexes with traditional interaction networks.
  • Reconstructing the human-virus structural interaction network.
  • Analyzing interface overlap, mimicry, and evolutionary rates.

Main Results:

  • Viral proteins mimic host-protein interfaces, competing with endogenous binding partners.
  • Mimicked endogenous interfaces are often transient and regulatory.
  • Viral interface mimicry can occur without sequence or structural similarity to host proteins.
  • Host-pathogen interfaces, especially overlapping ones, evolve faster than endogenous interfaces, indicating an evolutionary arms race.

Conclusions:

  • Host-pathogen protein-protein interactions exhibit distinct biophysical, functional, and evolutionary properties compared to endogenous interactions.
  • Structural analysis provides mechanistic insights into viral antagonism and host defense.
  • Understanding these differences is crucial for deciphering biological networks under conflict versus cooperation.