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3D domain swapping: A mechanism for oligomer assembly

Protein Science · 1995 · Vol. 4(12) · pp. 2455–2468

Melanie J. Bennett(University of California, Los Angeles)Michael P. Schlunegger(University of California, Los Angeles)David Eisenberg✉(University of California, Los Angeles)

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Abstract

3D domain swapping is a mechanism for forming oligomeric proteins from their monomers. In 3D domain swapping, one domain of a monomeric protein is replaced by the same domain from an identical protein chain. The result is an intertwined dimer or higher oligomer, with one domain of each subunit replaced by the identical domain from another subunit. The swapped "domain" can be as large as an entire tertiary globular domain, or as small as an alpha-helix or a strand of a beta-sheet. Examples of 3D domain swapping are reviewed that suggest domain swapping can serve as a mechanism for functional interconversion between monomers and oligomers, and that domain swapping may serve as a mechanism for evolution of some oligomeric proteins. Domain-swapped proteins present examples of a single protein chain folding into two distinct structures.

Protein Structure and Dynamics Enzyme Structure and Function RNA and protein synthesis mechanismsEGF-like domainHAMP domainOligomerDomain (mathematical analysis)Cyclic nucleotide-binding domainDimerProtein domainProtein subunitMonomerFolding (DSP implementation)

MeSH terms

Carrier ProteinsEndoribonucleasesModels, MolecularProtein KinasesProteinsRibonuclease, PancreaticInterleukin-5Granulocyte-Macrophage Colony-Stimulating FactorProtein Structure, SecondaryCell Cycle ProteinsCDC2-CDC28 KinasesMacromolecular Substances