2MAH
Solution structure of Smoothened
Summary for 2MAH
| Entry DOI | 10.2210/pdb2mah/pdb |
| NMR Information | BMRB: 19354 |
| Descriptor | Protein smoothened (1 entity in total) |
| Functional Keywords | smoothened, hedgehog, oncoprotein |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Cellular location | Membrane; Multi-pass membrane protein: P91682 |
| Total number of polymer chains | 1 |
| Total formula weight | 14881.30 |
| Authors | Rana, R.,Lee, H.,Zheng, J.J. (deposition date: 2013-07-09, release date: 2014-03-05, Last modification date: 2024-11-20) |
| Primary citation | Rana, R.,Carroll, C.E.,Lee, H.J.,Bao, J.,Marada, S.,Grace, C.R.,Guibao, C.D.,Ogden, S.K.,Zheng, J.J. Structural insights into the role of the Smoothened cysteine-rich domain in Hedgehog signalling. Nat Commun, 4:2965-2965, 2013 Cited by PubMed Abstract: Smoothened (Smo) is a member of the Frizzled (FzD) class of G-protein-coupled receptors (GPCRs), and functions as the key transducer in the Hedgehog (Hh) signalling pathway. Smo has an extracellular cysteine-rich domain (CRD), indispensable for its function and downstream Hh signalling. Despite its essential role, the functional contribution of the CRD to Smo signalling has not been clearly elucidated. However, given that the FzD CRD binds to the endogenous Wnt ligand, it has been proposed that the Smo CRD may bind its own endogenous ligand. Here we present the NMR solution structure of the Drosophila Smo CRD, and describe interactions between the glucocorticoid budesonide (Bud) and the Smo CRDs from both Drosophila and human. Our results highlight a function of the Smo CRD, demonstrating its role in binding to small-molecule modulators. PubMed: 24351982DOI: 10.1038/ncomms3965 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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