The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Two-State Allosteric Behavior in a Single-Domain Signaling Protein
Abstract
Protein actions are usually discussed in terms of static structures, but function requires motion. We find a strong correlation between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics. Using nuclear magnetic resonance relaxation, we characterized the motions of NtrC in three functional states: unphosphorylated (inactive), phosphorylated (active), and a partially active mutant. These dynamics are indicative of exchange between inactive and active conformations. Both states are populated in unphosphorylated NtrC, and phosphorylation shifts the equilibrium toward the active species. These results support a dynamic population shift between two preexisting conformations as the underlying mechanism of activation.
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Cites
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Dynamic personalities of proteins
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Self-citationThe role of dynamic conformational ensembles in biomolecular recognition
Boehr, D. D., Nussinov, R., & Wright, P. E. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.232 · Cited by 2,008
Conformational diversity and protein evolution – a 60-year-old hypothesis revisited
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Molecular Mechanisms of Two-Component Signal Transduction
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Metadata
- Authors
- Volkman, B. F., Lipson, D., Wemmer, D. E., & Kern, D.
- Venue
- Science
- Published
- 2001-03-23
- Volume
- 291
- Issue
- 5512
- Pages
- 2429-2433
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2053004995
- Cited by
- 593
- References
- 26
- FWCI
- 9.23
- Type
- journal article
- Language
- en
- Open access
- closed
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- Volkman, B. F., Lipson, D., Wemmer, D. E., & Kern, D. (2001). Two-State Allosteric Behavior in a Single-Domain Signaling Protein. Science. https://doi.org/10.1126/science.291.5512.2429
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
