title: Structural, evolutionary, and assembly principles of protein oligomerization.
abstract: In the protein universe, 30-50% of proteins self-assemble to form symmetrical complexes consisting of multiple copies of themselves, called homomers. The prevalence of homomers motivates us to review many of their properties. In Section 1, we describe the methods and challenges associated with quaternary structure inference-these methods are indeed at the basis of any analysis on homomers. In Section 2, we describe the morphological properties of homomers, as well as the database 3DComplex, which provides a taxonomy for both homomeric and heteromeric protein complexes. In Section 3, we review interface properties of homomeric complexes. In Section 4, we then present recent findings on the evolution of homomer interfaces, which we link in Section 5 to the evolution of homomers as entire entities. In Section 6, we discuss mechanisms involved in their assembly and how these mechanisms can be linked to evolution.
authors.affiliation: Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel. emmanuel.levy@weizmann.ac.il
authors.forename: Emmanuel D
authors.initials: ED
authors.lastname: Levy
authors.forename: Sarah
authors.initials: S
authors.lastname: Teichmann
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D019143:Evolution, Molecular; D020440:Gene Duplication; D006801:Humans; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*
chemical_list: D011506:Proteins