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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caption="1db1, resolution 1.8&Aring;" />
'''CRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN D'''<br />
'''CRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN D'''<br />
==Overview==
==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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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==
==Disease==
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==About this Structure==
==About this Structure==
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1DB1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with VDX as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DB1 OCA].
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1DB1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=VDX:'>VDX</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DB1 OCA].
==Reference==
==Reference==
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[[Category: Moras, D.]]
[[Category: Moras, D.]]
[[Category: Rochel, N.]]
[[Category: Rochel, N.]]
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[[Category: Wurtz, J.M.]]
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[[Category: Wurtz, J M.]]
[[Category: VDX]]
[[Category: VDX]]
[[Category: complex]]
[[Category: complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:30:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:14:47 2008''

Revision as of 10:14, 21 February 2008

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 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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