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Solution structure and dynamics of a de novo designed three-helix bundle protein
Open accessAbstract
Although de novo protein design is an important endeavor with implications for understanding protein folding, until now, structures have been determined for only a few 25- to 30-residue designed miniproteins. Here, the NMR solution structure of a complex 73-residue three-helix bundle protein, α 3 D, is reported. The structure of α 3 D was not based on any natural protein, and yet it shows thermodynamic and spectroscopic properties typical of native proteins. A variety of features contribute to its unique structure, including electrostatics, the packing of a diverse set of hydrophobic side chains, and a loop that incorporates common capping motifs. Thus, it is now possible to design a complex protein with a well defined and predictable three-dimensional structure.
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Citations
Cites
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
Crystal structure of an isoleucine-zipper trimer
Harbury, P. B., Kim, P. S., & Alber, T. (1994) · Nature · doi:10.1038/371080a0 · Cited by 472
Cited by
How fast-folding proteins fold
Lindorff-Larsen, K., Piana, S., Dror, R. O., & Shaw, D. E. (2011) · Science · doi:10.1126/science.1208351 · Cited by 1,980
The coming of age of de novo protein design
Huang, P.-S., Boyken, S. E., & Baker, D. (2016) · Nature · doi:10.1038/nature19946 · Cited by 1,478
Designing a 20-residue protein
Neidigh, J. W., Fesinmeyer, R. M., & Andersen, N. H. (2002) · Nature Structural Biology · doi:10.1038/nsb798 · Cited by 793
Native contacts determine protein folding mechanisms in atomistic simulations
Best, R. B., Hummer, G., & Eaton, W. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311599110 · Cited by 594
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Metadata
- Authors
- Walsh, S. T. R., Cheng, H., Bryson, J. W., Roder, H., & DeGrado, W. F.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1999-05-11
- Volume
- 96
- Issue
- 10
- Pages
- 5486-5491
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2170285690
- Cited by
- 220
- References
- 2
- FWCI
- 4.24
- Type
- journal article
- Language
- en
- Open access
- green
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- Walsh, S. T. R., Cheng, H., Bryson, J. W., Roder, H., & DeGrado, W. F. (1999). Solution structure and dynamics of a de novo designed three-helix bundle protein. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.96.10.5486
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