Premium
3D domain swapping: A mechanism for oligomer assembly
Author(s) -
Bennett Melanie J.,
Schlunegger Michael P.,
Eisenberg David
Publication year - 1995
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.5560041202
Subject(s) - egf like domain , hamp domain , oligomer , domain (mathematical analysis) , cyclic nucleotide binding domain , dimer , protein domain , protein subunit , monomer , folding (dsp implementation) , chemistry , protein folding , mechanism (biology) , b3 domain , biophysics , crystallography , peptide sequence , biology , dna binding domain , biochemistry , physics , gene , mathematical analysis , mathematics , organic chemistry , quantum mechanics , transcription factor , electrical engineering , engineering , polymer
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 α ‐helix or a strand of a β ‐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.