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Updated: May 11, 2026
11:27
X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Structural, evolutionary, and assembly principles of protein oligomerization
Emmanuel D Levy1, Sarah Teichmann
1Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel. emmanuel.levy@weizmann.ac.il
Summary
Approximately half of all proteins form symmetrical structures called homomers. This review covers homomer analysis, morphology, interfaces, and their evolution, assembly mechanisms, and evolutionary links.
Area of Science:
- Biochemistry
- Structural Biology
- Bioinformatics
Background:
- Proteins frequently self-assemble into symmetrical complexes known as homomers.
- Understanding homomer properties is crucial due to their prevalence (30-50% of proteins).
Purpose of the Study:
- To provide a comprehensive review of homomer properties.
- To discuss methods for quaternary structure inference.
- To explore the evolution and assembly of homomers.
Main Methods:
- Review of existing literature on protein quaternary structure inference.
- Analysis of morphological and interface properties of homomeric complexes.
- Examination of evolutionary data and assembly mechanisms.
Main Results:
- Detailed description of quaternary structure inference methods and challenges.
- Introduction to the 3DComplex database for protein complex taxonomy.
- Overview of homomer interface characteristics and evolutionary trends.
- Discussion on assembly mechanisms and their evolutionary implications.
Conclusions:
- Homomers represent a significant class of protein structures with diverse properties.
- Quaternary structure inference is fundamental to homomer analysis.
- The evolution and assembly of homomers are interconnected and influenced by interface properties.
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