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| | <StructureSection load='1r4r' size='340' side='right'caption='[[1r4r]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1r4r' size='340' side='right'caption='[[1r4r]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1r4r]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4R OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R4R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1r4r]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R4R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1glu|1glu]], [[1r4o|1r4o]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NR3C1 OR GRL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=1r4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4r OCA], [https://pdbe.org/1r4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r4r RCSB], [https://www.ebi.ac.uk/pdbsum/1r4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4r ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4r OCA], [http://pdbe.org/1r4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r4r RCSB], [http://www.ebi.ac.uk/pdbsum/1r4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r4r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GCR_RAT GCR_RAT]] Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Involved in chromatin remodeling. Plays a significant role in transactivation (By similarity).<ref>PMID:12917342</ref> | + | [https://www.uniprot.org/uniprot/GCR_RAT GCR_RAT] Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Involved in chromatin remodeling. Plays a significant role in transactivation (By similarity).<ref>PMID:12917342</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Freedman, L P]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Luisi, B F]] | + | [[Category: Freedman LP]] |
| - | [[Category: Otwinowski, Z]] | + | [[Category: Luisi BF]] |
| - | [[Category: Sigler, P B]] | + | [[Category: Otwinowski Z]] |
| - | [[Category: Xu, W X]] | + | [[Category: Sigler PB]] |
| - | [[Category: Yamamoto, K R]] | + | [[Category: Xu WX]] |
| - | [[Category: Glucocorticoid]]
| + | [[Category: Yamamoto KR]] |
| - | [[Category: Gr]]
| + | |
| - | [[Category: Ir3]]
| + | |
| - | [[Category: Protein-dna complex]]
| + | |
| - | [[Category: Steroid receptor]]
| + | |
| - | [[Category: Transcription-dna complex]]
| + | |
| Structural highlights
Function
GCR_RAT Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Involved in chromatin remodeling. Plays a significant role in transactivation (By similarity).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Two crystal structures of the glucocorticoid receptor DNA-binding domain complexed with DNA are reported. The domain has a globular fold which contains two Zn-nucleated substructures of distinct conformation and function. When it binds DNA, the domain dimerizes, placing the subunits in adjacent major grooves. In one complex, the DNA has the symmetrical consensus target sequence; in the second, the central spacing between the target's half-sites is larger by one base pair. This results in one subunit interacting specifically with the consensus target half-site and the other nonspecifically with a noncognate element. The DNA-induced dimer fixes the separation of the subunits' recognition surfaces so that the spacing between the half-sites becomes a critical feature of the target sequence's identity.
Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA.,Luisi BF, Xu WX, Otwinowski Z, Freedman LP, Yamamoto KR, Sigler PB Nature. 1991 Aug 8;352(6335):497-505. PMID:1865905[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hsiao PW, Fryer CJ, Trotter KW, Wang W, Archer TK. BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation. Mol Cell Biol. 2003 Sep;23(17):6210-20. PMID:12917342
- ↑ Luisi BF, Xu WX, Otwinowski Z, Freedman LP, Yamamoto KR, Sigler PB. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature. 1991 Aug 8;352(6335):497-505. PMID:1865905 doi:http://dx.doi.org/10.1038/352497a0
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