5uc1
From Proteopedia
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<StructureSection load='5uc1' size='340' side='right' caption='[[5uc1]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='5uc1' size='340' side='right' caption='[[5uc1]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5uc1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UC1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5uc1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hetga Hetga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UC1 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=486:11-(4-DIMETHYLAMINO-PHENYL)-17-HYDROXY-13-METHYL-17-PROP-1-YNYL-1,2,6,7,8,11,12,13,14,15,16,17-DODEC+AHYDRO-CYCLOPENTA[A]PHENANTHREN-3-ONE'>486</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=486:11-(4-DIMETHYLAMINO-PHENYL)-17-HYDROXY-13-METHYL-17-PROP-1-YNYL-1,2,6,7,8,11,12,13,14,15,16,17-DODEC+AHYDRO-CYCLOPENTA[A]PHENANTHREN-3-ONE'>486</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uc3|5uc3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5uc3|5uc3]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GW7_10599 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10181 HETGA])</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=5uc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uc1 OCA], [http://pdbe.org/5uc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5uc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uc1 ProSAT]</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=5uc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uc1 OCA], [http://pdbe.org/5uc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5uc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uc1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Glucocorticoid receptor beta (GRbeta) is associated with glucocorticoid resistance via dominant negative regulation of GRalpha. To better understand how GRbeta functions as a dominant negative inhibitor of GRalpha at a molecular level, we determined the crystal structure of the ligand binding domain of GRbeta complexed with antagonist RU-486. The structure reveals that RU-486 binds in the same ligand binding pocket as in GRalpha and the unique C-terminal amino acids of GRbeta are mostly disordered. Binding energy analysis suggests that these C-terminal residues of GRbeta do not contribute to RU-486 binding. Intriguingly, the GRbeta/RU-486 complex binds corepressor peptide with similar affinity as GRalpha/RU-486 complex, despite the lack of helix 12. Our biophysical and biochemical analysis reveals that in the presence of RU-486, GRbeta is found in a conformation that favors corepressor binding, potentially antagonizing GRalpha function. This study thus presents an unexpected molecular mechanism by which GRbeta could repress transcription. | ||
| + | |||
| + | Probing Dominant Negative Behavior of Glucocorticoid Receptor beta through a Hybrid Structural and Biochemical Approach.,Min J, Perera L, Krahn JM, Jewell CM, Moon AF, Cidlowski JA, Pedersen LC Mol Cell Biol. 2018 Feb 5. pii: MCB.00453-17. doi: 10.1128/MCB.00453-17. PMID:29437838<ref>PMID:29437838</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5uc1" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Glucocorticoid receptor|Glucocorticoid receptor]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Hetga]] | ||
[[Category: Min, J]] | [[Category: Min, J]] | ||
[[Category: Pedersen, L C]] | [[Category: Pedersen, L C]] | ||
[[Category: Hormone receptor]] | [[Category: Hormone receptor]] | ||
[[Category: Nuclear receptor]] | [[Category: Nuclear receptor]] | ||
Revision as of 06:19, 20 June 2018
Structural Analysis of Glucocorticoid Receptor beta Ligand Binding Domain Complexed with Glucocorticoid Antagonist RU-486: Implication of Helix 12 in Antagonism
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