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Cited by 764

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

3D domain swapping: A mechanism for oligomer assembly

Open access
Bennett, Melanie J., Schlunegger, Michael P., Eisenberg, David·1995·Protein Science

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 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.

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Metadata

Authors
Bennett, M. J., Schlunegger, M. P., & Eisenberg, D.
Venue
Protein Science
Publisher
Wiley
Published
1995-12
Volume
4
Issue
12
Pages
2455-2468
ISSN
  • 0961-8368 (ISSN-L)
  • 1469-896X
OpenAlex
W1978012062
Cited by
764
References
2
FWCI
9.83
Type
journal article
Language
en
Open access
green

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