protein complex
Definition
A protein complex is a stable assembly of two or more protein subunits that interact through non-covalent bonds to form a functional molecular machine. These multi-protein structures perform essential cellular functions including DNA replication, transcription, translation, signal transduction, and metabolic processes. Protein complexes can be homo-oligomeric (identical subunits) or hetero-oligomeric (different subunits), and their composition may be constitutive or dynamically regulated. Understanding protein complex architecture is crucial for elucidating cellular mechanisms, as many biological processes require coordinated action of multiple proteins. Disruption of protein complex assembly or stability often underlies disease pathology, making these structures important therapeutic targets in drug discovery.
Visualize protein complex in Nodes Bio
Researchers can visualize protein complexes as interconnected network nodes, where individual proteins are represented as nodes and their physical interactions as edges. Nodes Bio enables mapping of complex stoichiometry, identifying core versus peripheral components, and overlaying post-translational modifications or disease mutations onto complex structures. Users can integrate proteomics data with pathway information to understand how complexes function within broader cellular networks and identify potential drug targets.
Visualization Ideas:
- Protein-protein interaction networks showing complex subunit composition and binding interfaces
- Dynamic assembly networks illustrating temporal formation of complexes during cellular processes
- Disease mutation impact maps overlaying genetic variants onto protein complex structures
Example Use Case
A cancer researcher investigating the mTOR signaling pathway discovers that mTORC1 complex assembly is disrupted in treatment-resistant tumors. Using mass spectrometry-based proteomics, they identify altered protein-protein interactions between mTOR, Raptor, and mLST8 subunits. By visualizing the mTORC1 complex network alongside phosphoproteomics data, they reveal that a specific mutation prevents proper complex formation, leading to aberrant downstream signaling. This insight guides development of combination therapies targeting alternative nodes in the network to overcome resistance mechanisms.