The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Ligand-Binding PAS Domains in a Genomic, Cellular, and Structural Context
Open accessAbstract
Per-Arnt-Sim (PAS) domains occur in proteins from all kingdoms of life. In the bacterial kingdom, PAS domains are commonly positioned at the amino terminus of signaling proteins such as sensor histidine kinases, cyclic-di-GMP synthases/hydrolases, and methyl-accepting chemotaxis proteins. Although these domains are highly divergent at the primary sequence level, the structures of dozens of PAS domains across a broad section of sequence space have been solved, revealing a conserved three-dimensional architecture. An all-versus-all alignment of 63 PAS structures demonstrates that the PAS domain family forms structural clades on the basis of two principal variables: (a) topological location inside or outside the plasma membrane and (b) the class of small molecule that they bind. The binding of a chemically diverse range of small-molecule metabolites is a hallmark of the PAS domain family. PAS ligand binding either functions as a primary cue to initiate a cellular signaling response or provides the domain with the capacity to respond to secondary physical or chemical signals such as gas molecules, redox potential, or photons. This review synthesizes the current state of knowledge of the structural foundations and evolution of ligand recognition and binding by PAS domains.
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Cites
The Pfam protein families database
Finn, R. D., Mistry, J., Tate, J., Coggill, P., Heger, A., Pollington, J. E., Gavin, O. L., Gunasekaran, P., Ceric, G., Forslund, K., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp985 · Cited by 2,694
Mammalian Per-Arnt-Sim Proteins in Environmental Adaptation
McIntosh, B. E., Hogenesch, J. B., & Bradfield, C. A. (2010) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021909-135922 · Cited by 352
Artificial ligand binding within the HIF2α PAS-B domain of the HIF2 transcription factor
Scheuermann, T. H., Tomchick, D. R., Machius, M., Guo, Y., Bruick, R. K., & Gardner, K. H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808092106 · Cited by 301
Cited by
Structural integration in hypoxia-inducible factors
Wu, D., Potluri, N., Lu, J., Kim, Y., & Rastinejad, F. (2015) · Nature · doi:10.1038/nature14883 · Cited by 346
Allosteric inhibition of hypoxia inducible factor-2 with small molecules
Scheuermann, T. H., Li, Q., Ma, H.-W., Key, J., Zhang, L., Chen, R., Garcia, J. A., Naidoo, J., Longgood, J., Frantz, D. E., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1185 · Cited by 315
Suzuki, Y., Murray, S. L., Wong, K. H., Davis, M. A., & Hynes, M. J. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08067.x · Cited by 46
Tong, Y., Kaya, S. G., Russo, S., Rozeboom, H. J., Wijma, H. J., & Fraaije, M. W. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c12009 · Cited by 24
Bovier, E., Sellem, C. H., Humbert, A., & Sainsard-Chanet, A. (2014) · Eukaryotic Cell · doi:10.1128/ec.00172-13 · Cited by 16
Metadata
- Authors
- Henry, J. T., & Crosson, S.
- Venue
- Annual Review of Microbiology
- Publisher
- Annual Reviews
- Published
- 2011-10-13
- Volume
- 65
- Issue
- 1
- Pages
- 261-286
- ISSN
- 0066-4227 (ISSN-L)
- 1545-3251
- OpenAlex
- W2115273558
- Cited by
- 401
- References
- 3
- FWCI
- 1.31
- Type
- journal article
- Language
- en
- Open access
- green
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