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1lat

From Proteopedia

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[[Image:1lat.gif|left|200px]]
 
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{{Structure
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==GLUCOCORTICOID RECEPTOR MUTANT/DNA COMPLEX==
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|PDB= 1lat |SIZE=350|CAPTION= <scene name='initialview01'>1lat</scene>, resolution 1.900&Aring;
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<StructureSection load='1lat' size='340' side='right'caption='[[1lat]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1lat]] 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=1LAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LAT FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE= RAT GR AMINO ACIDS 440 TO 515 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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<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>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lat OCA], [https://pdbe.org/1lat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lat RCSB], [https://www.ebi.ac.uk/pdbsum/1lat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lat ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/la/1lat_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lat ConSurf].
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<div style="clear:both"></div>
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'''GLUCOCORTICOID RECEPTOR MUTANT/DNA COMPLEX'''
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==See Also==
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*[[Glucocorticoid receptor 3D structures|Glucocorticoid receptor 3D structures]]
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== References ==
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==Overview==
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<references/>
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Steroid receptors recognize bipartite targets composed of six base-pair half-sites. There are two canonical types of half-site which differ only in their central two base pairs. The crystal structure of an estrogen receptor-like DNA-binding domain bound to the wrong type of half-site (a glucocorticoid response element) reveals an interface that resembles the specific interfaces of the glucocorticoid receptor or estrogen receptor bound to their correct response elements. The underlying stereochemical defect that weakens the non-cognate interface is a difference in the helical geometry of the incorrect DNA half-site which prevents a side-chain contact and results in a gap which is filled by at least five additional fixed water sites, imposing a potential entropic burden on the stability of the interface.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1LAT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAT OCA].
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==Reference==
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The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex., Gewirth DT, Sigler PB, Nat Struct Biol. 1995 May;2(5):386-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7664096 7664096]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Gewirth DT]]
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[[Category: Gewirth, D T.]]
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[[Category: Sigler PB]]
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[[Category: Sigler, P B.]]
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[[Category: ZN]]
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[[Category: dna binding regulatory protein]]
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[[Category: glucocorticoid receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:39 2008''
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Current revision

GLUCOCORTICOID RECEPTOR MUTANT/DNA COMPLEX

PDB ID 1lat

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