1PDU
Ligand-binding domain of Drosophila orphan nuclear receptor DHR38
Summary for 1PDU
Entry DOI | 10.2210/pdb1pdu/pdb |
Descriptor | nuclear hormone receptor HR38 (2 entities in total) |
Functional Keywords | nuclear receptor, ligand-binding domain, hormone-growth factor receptor complex, hormone/growth factor receptor |
Biological source | Drosophila melanogaster (fruit fly) |
Cellular location | Nucleus: P49869 |
Total number of polymer chains | 2 |
Total formula weight | 56358.93 |
Authors | Baker, K.D.,Shewchuk, L.M.,Korlova, T.,Makishima, M.,Hassell, A.M.,Wisely, B.,Caravella, J.A.,Lambert, M.H.,Wilson, T.M.,Mangelsdorf, D.J. (deposition date: 2003-05-20, release date: 2003-06-10, Last modification date: 2024-02-14) |
Primary citation | Baker, K.D.,Shewchuk, L.M.,Korlova, T.,Makishima, M.,Hassell, A.M.,Wisely, B.,Caravella, J.A.,Lambert, M.H.,Reinking, J.L.,Krause, H.,Thummel, C.S.,Wilson, T.M.,Mangelsdorf, D.J. The Drosophila orphan nuclear receptor DHR38 mediates an atypical ecdysteroid signaling pathway. Cell(Cambridge,Mass.), 113:731-742, 2003 Cited by PubMed Abstract: Ecdysteroid pulses trigger the major developmental transitions during the Drosophila life cycle. These hormonal responses are thought to be mediated by the ecdysteroid receptor (EcR) and its heterodimeric partner Ultraspiracle (USP). We provide evidence for a second ecdysteroid signaling pathway mediated by DHR38, the Drosophila ortholog of the mammalian NGFI-B subfamily of orphan nuclear receptors. DHR38 also heterodimerizes with USP, and this complex responds to a distinct class of ecdysteroids in a manner that is independent of EcR. This response is unusual in that it does not involve direct binding of ecdysteroids to either DHR38 or USP. X-ray crystallographic analysis of DHR38 reveals the absence of both a classic ligand binding pocket and coactivator binding site, features that seem to be common to all NGFI-B subfamily members. Taken together, these data reveal the existence of a separate structural class of nuclear receptors that is conserved from fly to humans. PubMed: 12809604DOI: 10.1016/S0092-8674(03)00420-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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