3aun

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aun RCSB], [http://www.ebi.ac.uk/pdbsum/3aun PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aun RCSB], [http://www.ebi.ac.uk/pdbsum/3aun PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/VDR_RAT VDR_RAT]] Nuclear hormone receptor. Transcription factor that mediates the action of vitamin D3 by controlling the expression of hormone sensitive genes. Regulates transcription of hormone sensitive genes via its association with the WINAC complex, a chromatin-remodeling complex. Recruited to promoters via its interaction with the WINAC complex subunit BAZ1B/WSTF, which mediates the interaction with acetylated histones, an essential step for VDR-promoter association. Plays a central role in calcium homeostasis.<ref>PMID:17227670</ref> [[http://www.uniprot.org/uniprot/MED1_HUMAN MED1_HUMAN]] Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.<ref>PMID:9653119</ref> <ref>PMID:10406464</ref> <ref>PMID:12218053</ref> <ref>PMID:12037571</ref> <ref>PMID:11867769</ref> <ref>PMID:12556447</ref> <ref>PMID:14636573</ref> <ref>PMID:15471764</ref> <ref>PMID:15340084</ref> <ref>PMID:15989967</ref> <ref>PMID:16574658</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Kakuda, S.]]
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[[Category: Kakuda, S]]
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[[Category: Takimoto-Kamimura, M.]]
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[[Category: Takimoto-Kamimura, M]]
[[Category: Binding site]]
[[Category: Binding site]]
[[Category: Biphenyl compound]]
[[Category: Biphenyl compound]]

Revision as of 10:08, 25 December 2014

Crystal structure of the rat vitamin D receptor ligand binding domain complexed with YR335 and a synthetic peptide containing the NR2 box of DRIP 205

3aun, resolution 1.81Å

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