4dm8: Difference between revisions

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New page: '''Unreleased structure''' The entry 4dm8 is ON HOLD Authors: Osz, J., Br livet, Y., Peluso-Iltis, C., Cura, V., Eiler, S., Ruff, M., Bourguet, W., Rochel, N., Moras, D. Description: C...
 
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'''Unreleased structure'''


The entry 4dm8 is ON HOLD
==Crystal structure of RARb LBD in complex with 9cis retinoic acid==
<StructureSection load='4dm8' size='340' side='right'caption='[[4dm8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4dm8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DM8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=REA:RETINOIC+ACID'>REA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dm8 OCA], [https://pdbe.org/4dm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dm8 RCSB], [https://www.ebi.ac.uk/pdbsum/4dm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dm8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RARB_HUMAN RARB_HUMAN] Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function.<ref>PMID:12554770</ref>


Authors: Osz, J., Br livet, Y., Peluso-Iltis, C., Cura, V., Eiler, S., Ruff, M., Bourguet, W., Rochel, N., Moras, D.
==See Also==
 
*[[Retinoic acid receptor 3D structures|Retinoic acid receptor 3D structures]]
Description: Crystal structure of RARb LBD in complex with 9cis retinoic acid
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bourguet W]]
[[Category: Br livet Y]]
[[Category: Cura V]]
[[Category: Eiler S]]
[[Category: Moras D]]
[[Category: Osz J]]
[[Category: Peluso-Iltis C]]
[[Category: Rochel N]]
[[Category: Ruff M]]

Latest revision as of 13:50, 1 March 2024

Crystal structure of RARb LBD in complex with 9cis retinoic acidCrystal structure of RARb LBD in complex with 9cis retinoic acid

Structural highlights

4dm8 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RARB_HUMAN Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function.[1]

See Also

References

  1. Hauksdottir H, Farboud B, Privalsky ML. Retinoic acid receptors beta and gamma do not repress, but instead activate target gene transcription in both the absence and presence of hormone ligand. Mol Endocrinol. 2003 Mar;17(3):373-85. Epub 2002 Dec 23. PMID:12554770 doi:10.1210/me.2002-0340

4dm8, resolution 2.30Å

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