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Related Concept Videos

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-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 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: Jun 27, 2026

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

Cataloguing the HIV type 1 human protein interaction network.

Roger G Ptak1, William Fu, Brigitte E Sanders-Beer

  • 1Department of Infectious Disease Research, Southern Research Institute, 431 Aviation Way, Frederick, MD 21701, USA. ptak@southernresearch.org

AIDS Research and Human Retroviruses
|November 26, 2008
PubMed
Summary
This summary is machine-generated.

A new database catalogs over 2500 human-HIV-1 protein interactions from PubMed, revealing 37% of human proteins interact with multiple HIV-1 proteins, aiding therapeutic development.

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Area of Science:

  • Virology
  • Molecular Biology
  • Bioinformatics

Background:

  • Numerous interactions between Human Immunodeficiency Virus type 1 (HIV-1) and human proteins exist in scientific literature.
  • A lack of a centralized, accessible resource hinders efficient review of these interactions.

Purpose of the Study:

  • To create a comprehensive, publicly accessible database of all published HIV-1 and human protein interactions.
  • To facilitate research into HIV-1 replication, pathogenesis, and the development of interventions.

Main Methods:

  • Systematic review of HIV-related articles in PubMed.
  • Development of a database including protein names, Entrez GeneIDs, RefSeq accession numbers, interaction descriptions, and PubMed IDs.
  • Data extraction and preliminary analysis of interaction types and frequencies.

Main Results:

  • Identified 1448 human proteins interacting with HIV-1, comprising 2589 unique interactions.
  • Found 32% direct physical interactions and 68% indirect interactions.
  • Discovered 37% of human proteins interact with multiple HIV-1 proteins, with notable interactions involving Tat and envelope proteins.

Conclusions:

  • The created database is a unique, continuously updated resource for HIV-1 research.
  • This resource supports understanding HIV-1 pathogenesis and accelerates the development of therapeutics and vaccines.
  • The database is accessible via NCBI and cross-linked with other relevant databases.