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1PDU

Ligand-binding domain of Drosophila orphan nuclear receptor DHR38

Summary for 1PDU
Entry DOI10.2210/pdb1pdu/pdb
Descriptornuclear hormone receptor HR38 (2 entities in total)
Functional Keywordsnuclear receptor, ligand-binding domain, hormone-growth factor receptor complex, hormone/growth factor receptor
Biological sourceDrosophila melanogaster (fruit fly)
Cellular locationNucleus: P49869
Total number of polymer chains2
Total formula weight56358.93
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 citationBaker, 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: 12809604
DOI: 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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数据于2024-11-06公开中

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