The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Domain swapping: entangling alliances between proteins.
Open accessAbstract
The comparison of monomeric and dimeric diphtheria toxin (DT) reveals a mode for protein association which we call domain swapping. The structure of dimeric DT has been extensively refined against data to 2.0-A resolution and a three-residue loop has been corrected as compared with our published 2.5-A-resolution structure. The monomeric DT structure has also been determined, at 2.3-A resolution. Monomeric DT is a Y-shaped molecule with three domains: catalytic (C), transmembrane (T), and receptor binding (R). Upon freezing in phosphate buffer, DT forms a long-lived, metastable dimer. The protein chain tracing discloses that upon dimerization an unprecedented conformational rearrangement occurs: the entire R domain from each molecule of the dimer is exchanged for the R domain from the other. This involves breaking the noncovalent interactions between the R domain and the C and T domains, rotating the R domain by 180 degrees with atomic movements up to 65 A, and re-forming the same noncovalent interactions between the R domain and the C and T domains of the other chain of the dimer. This conformational transition explains the long life and metastability of the DT dimer. Several other intertwined, dimeric protein structures satisfy our definition of domain swapping and suggest that domain swapping may be the molecular mechanism for evolution of these oligomers and possibly of oligomeric proteins in general.
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Cites
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Cited by
Detecting Protein Function and Protein-Protein Interactions from Genome Sequences
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Self-citationAgeing and vision: structure, stability and function of lens crystallins
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3D domain swapping: As domains continue to swap
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Self-citationFolding funnels, binding funnels, and protein function
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Folding funnels and binding mechanisms
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Metadata
- Authors
- Bennett, M. J., Choe, S., & Eisenberg, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1994-04-12
- Volume
- 91
- Issue
- 8
- Pages
- 3127-3131
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2036454087
- Cited by
- 532
- References
- 30
- FWCI
- 6.62
- Type
- journal article
- Language
- en
- Open access
- green
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