The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Surface Sites for Engineering Allosteric Control in Proteins
Open accessAbstract
Statistical analyses of protein families reveal networks of coevolving amino acids that functionally link distantly positioned functional surfaces. Such linkages suggest a concept for engineering allosteric control into proteins: The intramolecular networks of two proteins could be joined across their surface sites such that the activity of one protein might control the activity of the other. We tested this idea by creating PAS-DHFR, a designed chimeric protein that connects a light-sensing signaling domain from a plant member of the Per/Arnt/Sim (PAS) family of proteins with Escherichia coli dihydrofolate reductase (DHFR). With no optimization, PAS-DHFR exhibited light-dependent catalytic activity that depended on the site of connection and on known signaling mechanisms in both proteins. PAS-DHFR serves as a proof of concept for engineering regulatory activities into proteins through interface design at conserved allosteric sites.
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Cites
Dynamic personalities of proteins
Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545
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Self-citationStructure and Signaling Mechanism of Per-ARNT-Sim Domains
Möglich, A., Ayers, R. A., & Moffat, K. (2009) · Structure · doi:10.1016/j.str.2009.08.011 · Cited by 531
Structure and function of plant photoreceptors
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Metadata
- Authors
- Lee, J., Natarajan, M., Nashine, V. C., Socolich, M., Vo, T., Russ, W. P., Benkovic, S. J., & Ranganathan, R.
- Venue
- Science
- Published
- 2008-10-17
- Volume
- 322
- Issue
- 5900
- Pages
- 438-442
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2013726100
- Cited by
- 344
- References
- 1
- FWCI
- 9.80
- Type
- journal article
- Language
- en
- Open access
- green
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- Lee, J., Natarajan, M., Nashine, V. C., Socolich, M., Vo, T., Russ, W. P., Benkovic, S. J., & Ranganathan, R. (2008). Surface Sites for Engineering Allosteric Control in Proteins. Science. https://doi.org/10.1126/science.1159052
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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