Protein design by fusion: implications for protein structure prediction and evolution
SCIE
SCOPUS
- Title
- Protein design by fusion: implications for protein structure prediction and evolution
- Authors
- Skorupka, K; Han, SK; Nam, HJ; Kim, S; Faham, S
- Date Issued
- 2013-12
- Publisher
- International Union of Crystallography
- Abstract
- Domain fusion is a useful tool in protein design. Here, the structure of a fusion of the heterodimeric flagella-assembly proteins FliS and FliC is reported. Although the ability of the fusion protein to maintain the structure of the heterodimer may be apparent, threading-based structural predictions do not properly fuse the heterodimer. Additional examples of naturally occurring heterodimers that are homologous to full-length proteins were identified. These examples highlight that the designed protein was engineered by the same tools as used in the natural evolution of proteins and that heterodimeric structures contain a wealth of information, currently unused, that can improve structural predictions.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/9287
- DOI
- 10.1107/S0907444913022701
- ISSN
- 0907-4449
- Article Type
- Article
- Citation
- Acta Crystallographica Section D, vol. 69, no. 12, page. 2451 - 2460, 2013-12
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