1db1

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{{STRUCTURE_1db1| PDB=1db1 | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN D'''
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===CRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN D===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Wurtz, J M.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:45:58 2008''

Revision as of 19:46, 30 June 2008

Image:1db1.png


PDB ID 1db1

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1db1, resolution 1.80Å ()
Ligands:
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



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

Publication Abstract from PubMed

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 Structure

1DB1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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