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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MolProbity : all-atom structure validation for macromolecular crystallography
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Vertebrate Smoothened functions at the primary cilium
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Patched acts catalytically to suppress the activity of Smoothened
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Cited by
G protein-coupled receptors: structure- and function-based drug discovery
Yang, D., Zhou, Q., Labroska, V., Qin, S., Darbalaei, S., Wu, Y., Yuliantie, E., Xie, L., Tao, H., Cheng, J., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00435-w · Cited by 632
Structure of class B GPCR corticotropin-releasing factor receptor 1
Hollenstein, K., Kean, J., Bortolato, A., Cheng, R. K. Y., Doré, A. S., Jazayeri, A., Cooke, R. M., Weir, M., & Marshall, F. H. (2013) · Nature · doi:10.1038/nature12357 · Cited by 416
Cellular Cholesterol Directly Activates Smoothened in Hedgehog Signaling
Huang, P., Nedelcu, D., Watanabe, M., Jao, C., Kim, Y., Liu, J., & Salic, A. (2016) · Cell · doi:10.1016/j.cell.2016.08.003 · Cited by 377
Identification of recurrent SMO and BRAF mutations in ameloblastomas
Sweeney, R. T., McClary, A. C., Myers, B. R., Biscocho, J., Neahring, L., Kwei, K. A., Qu, K., Gong, X., Ng, T., Jones, C. D., et al. (2014) · Nature Genetics · doi:10.1038/ng.2986 · Cited by 366
Allosteric Modulation as a Unifying Mechanism for Receptor Function and Regulation
Changeux, J.-P., & Christopoulos, A. (2016) · Cell · doi:10.1016/j.cell.2016.08.015 · Cited by 336
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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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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