The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Structure of the human smoothened receptor bound to an antitumour agent
Open accessAbstract
The smoothened (SMO) receptor, a key signal transducer in the hedgehog signalling pathway, is responsible for the maintenance of normal embryonic development and is implicated in carcinogenesis. It is classified as a class frizzled (class F) G-protein-coupled receptor (GPCR), although the canonical hedgehog signalling pathway involves the GLI transcription factors and the sequence similarity with class A GPCRs is less than 10%. Here we report the crystal structure of the transmembrane domain of the human SMO receptor bound to the small-molecule antagonist LY2940680 at 2.5 Å resolution. Although the SMO receptor shares the seven-transmembrane helical fold, most of the conserved motifs for class A GPCRs are absent, and the structure reveals an unusually complex arrangement of long extracellular loops stabilized by four disulphide bonds. The ligand binds at the extracellular end of the seven-transmembrane-helix bundle and forms extensive contacts with the loops.
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Patched acts catalytically to suppress the activity of Smoothened
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Discovery of new GPCR ligands to illuminate new biology
Roth, B. L., Irwin, J. J., & Shoichet, B. K. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2490 · Cited by 94
Self-citationFusion protein strategies for cryo-EM study of G protein-coupled receptors
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Metadata
- Authors
- Wang, C., Wu, H., Katritch, V., Han, G. W., Huang, X.-P., Liu, W., Siu, F. Y., Roth, B. L., Cherezov, V., & Stevens, R. C.
- Venue
- Nature
- Published
- 2013-05
- Volume
- 497
- Issue
- 7449
- Pages
- 338-343
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2036833206
- Cited by
- 464
- References
- 7
- FWCI
- 30.26
- Type
- journal article
- Language
- en
- Open access
- green
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- Wang, C., Wu, H., Katritch, V., Han, G. W., Huang, X.-P., Liu, W., Siu, F. Y., Roth, B. L., Cherezov, V., & Stevens, R. C. (2013). Structure of the human smoothened receptor bound to an antitumour agent. Nature. https://doi.org/10.1038/nature12167
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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).
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