1db1: Difference between revisions

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[[Image:1db1.~~gif~~|left|200px]]

[[Image:1db1.png|left|200px]]

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

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

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_10678179}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10678179 is the PubMed ID number.

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==About this Structure==

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[[Category: Wurtz, J M.]]

[[Category: Complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:38:50 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:45:58 2008''

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-[[Image:1db1.gif|left|200px]]
+{{Seed}}
+[[Image:1db1.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1db1|  PDB=1db1  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN D'''
+===CRYSTAL STRUCTURE OF THE NUCLEAR RECEPTOR FOR VITAMIN D COMPLEXED TO VITAMIN D===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10678179}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10678179 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10678179}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Wurtz, J M.]]
 [[Category: Complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:38:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:45:58 2008''