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1db1

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(New page: 200px<br /> <applet load="1db1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1db1, resolution 1.8&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:24, 12 November 2007

Image:1db1.gif

1db1, resolution 1.8Å

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

Contents

Overview

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.

Disease

Known diseases associated with this structure: Osteoporosis, involutional, 166710 (1) OMIM:[601769], Rickets, vitamin D-resistant, type IIA OMIM:[601769]

About this Structure

1DB1 is a Single protein structure of sequence from Homo sapiens with VDX as ligand. 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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