2hcd: Difference between revisions
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'''Crystal structure of the ligand binding domain of the Vitamin D nuclear receptor in complex with Gemini and a coactivator peptide''' | '''Crystal structure of the ligand binding domain of the Vitamin D nuclear receptor in complex with Gemini and a coactivator peptide''' | ||
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[[Category: Moras, D.]] | [[Category: Moras, D.]] | ||
[[Category: Rochel, N.]] | [[Category: Rochel, N.]] | ||
[[Category: | [[Category: Alpha helical sandwich]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:07:12 2008'' | |||
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Revision as of 06:07, 4 May 2008
Crystal structure of the ligand binding domain of the Vitamin D nuclear receptor in complex with Gemini and a coactivator peptide
OverviewOverview
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 StructureAbout this Structure
2HCD is a Protein complex structure of sequences from Danio rerio. Full crystallographic information is available from OCA.
ReferenceReference
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 Sun May 4 06:07:12 2008