1db1

File:1db1.png

spinqualitylabelsall models PDB ID 1db1 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
1db1, resolution 1.80Å ()
Ligands:
Structural annotation: Resources: CATH : 1Db1A00 InterPro : Ipr000324, Ipr001723, Ipr000536, Ipr013088, Ipr001628, Ipr008946 Pfam : PF00104 SCOP : d1db1a_ UniProt : P11473
Functional annotation: Cellular component: nucleus Biological process: signal transduction intestinal absorption multicellular organismal development organ morphogenesis skeletal development negative regulation of transcription transcription calcium ion transport cellular calcium ion homeostasis regulation of transcription, DNA-dependent Molecular function: transcription factor activity receptor activity sequence-specific DNA binding metal ion binding protein binding vitamin D3 receptor activity ligand-dependent nuclear receptor activity transcription regulator activity steroid hormone receptor activity DNA binding zinc ion binding
Evolutionary conservation: Toggle Conservation Colors: Rows = identical sequences: Further Information: Caveats, Explanation, Complete Results at ConSurfDB
Resources:	FirstGlance, OCA, RCSB, PDBsum
Coordinates:	save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN DCRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN D

Publication Abstract from PubMed

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The action of 1 alpha, 25-dihydroxyvitamin D3 is mediated by its nuclear receptor (VDR), a ligand-dependent transcription regulator. We report the 1.8 A resolution crystal structure of the complex between a VDR ligand-binding domain (LBD) construct lacking the highly variable VDR-specific insertion domain and vitamin D. The construct exhibits the same binding affinity for vitamin D and transactivation ability as the wild-type protein, showing that the N-terminal part of the LBD is essential for its structural and functional integrity while the large insertion peptide is dispensable. The structure reveals the active conformation of the bound ligand and allows understanding of the different binding properties of some synthetic analogs.

The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand., Rochel N, Wurtz JM, Mitschler A, Klaholz B, Moras D, Mol Cell. 2000 Jan;5(1):173-9. PMID:10678179

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this StructureAbout this Structure

1db1 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See AlsoSee Also

• Vitamin D receptor