We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2hcd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
The crystal structure of the ligand binding domain (LBD) of the wild-type, Vitamin D receptor (VDR) of zebrafish bound to Gemini, a synthetic agonist, ligand with two identical side chains branching at carbon 20 reveals a, ligand-dependent structural rearrangement of the ligand binding pocket, (LBP). The rotation of a Leu side chain opens the access to a channel that, can accommodate the second side chain of the ligand. The 25% increase of, the LBP's volume does not alter the essential agonist features of VDR. The, possibility to adapt the LBP to novel ligands with different chemistry, and/or structure opens new perspectives in the design of more specifically, targeted ligands.
+
The crystal structure of the ligand binding domain (LBD) of the wild-type Vitamin D receptor (VDR) of zebrafish bound to Gemini, a synthetic agonist ligand with two identical side chains branching at carbon 20 reveals a ligand-dependent structural rearrangement of the ligand binding pocket (LBP). The rotation of a Leu side chain opens the access to a channel that can accommodate the second side chain of the ligand. The 25% increase of the LBP's volume does not alter the essential agonist features of VDR. The possibility to adapt the LBP to novel ligands with different chemistry and/or structure opens new perspectives in the design of more specifically targeted ligands.
==About this Structure==
==About this Structure==
Line 19: Line 19:
[[Category: alpha helical sandwich]]
[[Category: alpha helical sandwich]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:27:03 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:40:24 2008''

Revision as of 15:40, 21 February 2008

Image:2hcd.jpg

2hcd, resolution 2.6Å

Drag the structure with the mouse to rotate

Crystal structure of the ligand binding domain of the Vitamin D nuclear receptor in complex with Gemini and a coactivator peptide

Overview

The crystal structure of the ligand binding domain (LBD) of the wild-type Vitamin D receptor (VDR) of zebrafish bound to Gemini, a synthetic agonist ligand with two identical side chains branching at carbon 20 reveals a ligand-dependent structural rearrangement of the ligand binding pocket (LBP). The rotation of a Leu side chain opens the access to a channel that can accommodate the second side chain of the ligand. The 25% increase of the LBP's volume does not alter the essential agonist features of VDR. The possibility to adapt the LBP to novel ligands with different chemistry and/or structure opens new perspectives in the design of more specifically targeted ligands.

About this Structure

2HCD is a Protein complex structure of sequences from Danio rerio with as ligand. Full crystallographic information is available from OCA.

Reference

Adaptability of the Vitamin D nuclear receptor to the synthetic ligand Gemini: remodelling the LBP with one side chain rotation., Ciesielski F, Rochel N, Moras D, J Steroid Biochem Mol Biol. 2007 Mar;103(3-5):235-42. Epub 2007 Jan 10. PMID:17218092

Page seeded by OCA on Thu Feb 21 17:40:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hcd"
Personal tools