2hc4

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{{STRUCTURE_2hc4| PDB=2hc4 | SCENE= }}
{{STRUCTURE_2hc4| PDB=2hc4 | SCENE= }}
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'''Crystal structure of the LBD of VDR of Danio rerio in complex with calcitriol'''
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===Crystal structure of the LBD of VDR of Danio rerio in complex with calcitriol===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17218092 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17218092}}
==About this Structure==
==About this Structure==
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[[Category: Rochel, N.]]
[[Category: Rochel, N.]]
[[Category: Alpha helical sandwich]]
[[Category: Alpha helical sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:06:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:07:09 2008''

Revision as of 10:07, 29 July 2008

Image:2hc4.png

Template:STRUCTURE 2hc4

Crystal structure of the LBD of VDR of Danio rerio in complex with calcitriol

Template:ABSTRACT PUBMED 17218092

About this Structure

2HC4 is a Protein complex structure of sequences from Danio rerio. 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 Tue Jul 29 13:07:09 2008

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