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Related Concept Videos

Protein Complex Assembly02:41

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 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...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
Protein Complex Assembly02:41

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 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...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

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Related Experiment Video

Updated: Jun 7, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Assembly reflects evolution of protein complexes.

Emmanuel D Levy1, Elisabetta Boeri Erba, Carol V Robinson

  • 1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK. homomers@mrc-lmb.cam.ac.uk

Nature
|June 20, 2008
PubMed
Summary
This summary is machine-generated.

Protein homomer assembly and evolution share conserved pathways. This study reveals that protein quaternary structure evolution mirrors cellular assembly, enabling prediction from crystal structures.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Evolutionary Biology

Background:

  • Homomers, formed by self-interacting protein units, are crucial for cellular functions like allostery.
  • Mis-assembly of homomers is linked to various diseases, highlighting their structural importance.
  • Despite their prevalence (50-70% of known quaternary states), homomer evolution and assembly mechanisms are poorly understood.

Purpose of the Study:

  • To investigate the evolutionary conservation of homomer quaternary structures.
  • To elucidate the relationship between homomer evolutionary pathways and their in-cell assembly processes.
  • To develop a predictive model for protein complex evolution and assembly based on structural data.

Main Methods:

  • Analysis of over 5,000 unique atomic structures.
  • Comparative analysis of protein families to assess quaternary structure conservation.
  • Perturbation of subunit interfaces and mass spectrometry to study complex assembly pathways.

Main Results:

  • Homomer quaternary structure is conserved in over 70% of protein pairs with ≥30% sequence identity.
  • Well-defined evolutionary pathways exist for proteins transitioning between quaternary structure types.
  • In-cell (dis)assembly pathways were shown to mimic evolutionary pathways.

Conclusions:

  • Protein evolution and assembly pathways are molecularly analogous, mirroring Haeckel's developmental paradigm.
  • The study provides a model for predicting protein complex evolution and assembly from crystal structures.
  • Understanding these conserved mechanisms offers insights into disease and potential for designing novel molecular machines.