The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Design of three-dimensional domain-swapped dimers and fibrous oligomers
Open accessAbstract
Three-dimensional (3D) domain-swapped proteins are intermolecularly folded analogs of monomeric proteins; both are stabilized by the identical interactions, but the individual domains interact intramolecularly in monomeric proteins, whereas they form intermolecular interactions in 3D domain-swapped structures. The structures and conditions of formation of several domain-swapped dimers and trimers are known, but the formation of higher order 3D domain-swapped oligomers has been less thoroughly studied. Here we contrast the structural consequences of domain swapping from two designed three-helix bundles: one with an up-down-up topology, and the other with an up-down-down topology. The up-down-up topology gives rise to a domain-swapped dimer whose structure has been determined to 1.5 Å resolution by x-ray crystallography. In contrast, the domain-swapped protein with an up-down-down topology forms fibrils as shown by electron microscopy and dynamic light scattering. This demonstrates that design principles can predict the oligomeric state of 3D domain-swapped molecules, which should aid in the design of domain-swapped proteins and biomaterials.
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Citations
Cites
A Buried Polar Interaction Imparts Structural Uniqueness in a Designed Heterodimeric Coiled Coil
Lumb, K. J., & Kim, P. S. (1995) · Biochemistry · doi:10.1021/bi00027a013 · Cited by 266
Cited by
3D domain swapping: As domains continue to swap
Liu, Y., & Eisenberg, D. (2002) · Protein Science · doi:10.1110/ps.0201402 · Cited by 684
Self-citationSun, Z., Diaz, Z., Fang, X., Hart, M. P., Chesi, A., Shorter, J., & Gitler, A. D. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000614 · Cited by 458
Chemically Controlled Protein Assembly: Techniques and Applications
Fegan, A., White, B., Carlson, J. C. T., & Wagner, C. R. (2010) · Chemical Reviews · doi:10.1021/cr8002888 · Cited by 294
Rational Design of a Reversible pH-Responsive Switch for Peptide Self-Assembly
Zimenkov, Y., Dublin, S. N., Ni, R., Tu, R. S., Breedveld, V., Apkarian, R. P., & Conticello, V. P. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0605974 · Cited by 212
Design of a Selective Metal Ion Switch for Self-Assembly of Peptide-Based Fibrils
Dublin, S. N., & Conticello, V. P. (2008) · Journal of the American Chemical Society · doi:10.1021/ja0775016 · Cited by 156
Metadata
- Authors
- Ogihara, N. L., Ghirlanda, G., Bryson, J. W., Gingery, M., DeGrado, W. F., & Eisenberg, D.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-02-13
- Volume
- 98
- Issue
- 4
- Pages
- 1404-1409
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2022923144
- Cited by
- 183
- References
- 1
- FWCI
- 3.15
- Type
- journal article
- Language
- en
- Open access
- green
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- Ogihara, N. L., Ghirlanda, G., Bryson, J. W., Gingery, M., DeGrado, W. F., & Eisenberg, D. (2001). Design of three-dimensional domain-swapped dimers and fibrous oligomers. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.98.4.1404
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