Intertwined associations in structures of homooligomeric proteins.

TitleIntertwined associations in structures of homooligomeric proteins.
Publication TypeJournal Article
Year of Publication2013
AuthorsMackinnon, S. S., Malevanets A., and Wodak S. J.
JournalStructure
Volume21
Issue4
Pagination638-49
Date Published2013 Apr 2
ISSN1878-4186
KeywordsAmino Acid Sequence, Databases, Protein, Models, Molecular, Molecular Sequence Data, Multiprotein Complexes, Protein Conformation, Protein Subunits, Proteomics, Sequence Homology
Abstract

Intertwined homo-oligomers are complexes comprising identical protein subunits, where small segments or compact protein substructures (domains) are exchanged between the subunits. Using a formal definition of intertwined homo-oligomers, we survey the Protein Data Bank for all such complexes. Results show that intertwining occurs in 13,442 (24%) of all surveyed structures. A majority (∼72%) exchanges one contiguous chain segment of varying length. Another ∼10%, exchange structural domains, and the remaining ∼20% display complex intertwining topologies. Smaller proteins are more often intertwined, and intertwining is dominant in solution homodimers. These findings and analyses of various properties of the major category of intertwined complexes, their interfaces and quaternary context, support the physiological role of intertwining in promoting homooligomer stability. Furthermore, the number of different intertwining modes observed in families of related proteins is limited, and likely specific to the protein fold. These findings yield unique insights into the role of intertwining in homomeric association.

DOI10.1016/j.str.2013.01.019
Alternate JournalStructure
PubMed ID23523426
Grant List / / Canadian Institutes of Health Research / Canada
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