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Protein Complexes with Interchangeable Parts

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 Parts

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 Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Protein-protein Interfaces

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 Interfaces

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...

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Related Experiment Video

Updated: Jun 6, 2026

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

Published on: April 20, 2018

BISC: binary subcomplexes in proteins database.

Thomas Juettemann¹, Dietlind L Gerloff

¹School of Biology, University of Edinburgh, Edinburgh EH9 3JJ, UK.

Nucleic Acids Research

|November 18, 2010

Summary

The Binary Subcomplexes in Proteins database (BISC) integrates structural and functional genomics data for protein-protein interactions (PPIs). This resource aids in validating potential PPIs and identifying false positives in existing databases.

Area of Science:

Biochemistry
Structural Biology
Bioinformatics

Background:

Protein-protein interactions (PPIs) are crucial for cellular functions.
Existing PPI databases often lack integrated structural and functional genomics perspectives.
Characterizing binary subcomplexes requires bridging structural and functional data.

Purpose of the Study:

To introduce the Binary Subcomplexes in Proteins database (BISC).
To provide a unified resource for structural and functional genomics data on binary protein interactions.
To offer tools for validating postulated PPIs and identifying potential false positives.

Main Methods:

Integration of data from major functional genomics PPI databases (BioGRID, IntAct, HPRD).
Inclusion of structurally characterized and modellable binary protein-protein interactions.

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Last Updated: Jun 6, 2026

Split-BioID — Proteomic Analysis of Context-specific Protein Complexes in Their Native Cellular Environment

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Published on: April 20, 2018

The MultiBac Protein Complex Production Platform at the EMBL

The MultiBac Protein Complex Production Platform at the EMBL

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High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

High-Resolution Complexome Profiling by Cryoslicing BN-MS Analysis

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Development of web services for inspecting modelled protein-protein interaction interfaces.

Main Results:

BISC provides a structural perspective on binary subcomplexes.
The database links structural information with functional genomics data.
Web services enable the investigation of hypothetical protein-protein interaction interfaces.

Conclusions:

BISC serves as a valuable resource for researchers in structural biology and functional genomics.
The database can help improve the accuracy of PPI data by identifying false positives.
BISC facilitates a deeper understanding of direct physical interactions between proteins.