1fd0

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[[Image:1fd0.png|left|200px]]
 
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{{STRUCTURE_1fd0| PDB=1fd0 | SCENE= }}
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==ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254==
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<StructureSection load='1fd0' size='340' side='right'caption='[[1fd0]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fd0]] is a 1 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=1FD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FD0 FirstGlance]. <br>
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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]] 1.38&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=254:6-[HYDROXYIMINO-(5,5,8,8-TETRAMETHYL-5,6,7,8-TETRAHYDRO-NAPHTALEN-2-YL)-METHYL]-NAPHTALENE-2-CARBOXYLIC+ACID'>254</scene>, <scene name='pdbligand=LMU:DODECYL-ALPHA-D-MALTOSIDE'>LMU</scene></td></tr>
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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=1fd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fd0 OCA], [https://pdbe.org/1fd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fd0 RCSB], [https://www.ebi.ac.uk/pdbsum/1fd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fd0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RARG_HUMAN RARG_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 RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function (By similarity).
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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/fd/1fd0_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=1fd0 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Hydrogen bonds between polarized atoms play a crucial role in protein interactions and are often used in drug design, which usually neglects the potential of C-H...O hydrogen bonds. The 1.4 A resolution crystal structure of the ligand binding domain of the retinoic acid receptor RARgamma complexed with the retinoid SR11254 reveals several types of C-H...O hydrogen bonds. A striking example is the hydroxyl group of the ligand that acts as an H bond donor and acceptor, leading to a synergy between classical and C-H...O hydrogen bonds. This interaction introduces both specificity and affinity within the hydrophobic ligand pocket. The similarity of intraprotein and protein-ligand C-H...O interactions suggests that such bonds should be considered in rational drug design approaches.
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===ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254===
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C-H...O hydrogen bonds in the nuclear receptor RARgamma--a potential tool for drug selectivity.,Klaholz B, Moras D Structure. 2002 Sep;10(9):1197-204. PMID:12220491<ref>PMID:12220491</ref>
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{{ABSTRACT_PUBMED_12220491}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 1fd0" style="background-color:#fffaf0;"></div>
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[[1fd0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FD0 OCA].
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==See Also==
==See Also==
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*[[Retinoic acid receptor|Retinoic acid receptor]]
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*[[Retinoic acid receptor 3D structures|Retinoic acid receptor 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:012220491</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Klaholz, B P.]]
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[[Category: Large Structures]]
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[[Category: Moras, D.]]
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[[Category: Klaholz BP]]
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[[Category: SPINE, Structural Proteomics in Europe.]]
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[[Category: Moras D]]
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[[Category: Antiparallel alpha-helical sandwich fold]]
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[[Category: Ch...o hydrogen bond]]
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[[Category: Drug design]]
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[[Category: Gene regulation]]
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[[Category: Isotype selectivity]]
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[[Category: Retinoid ligand complex]]
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[[Category: Spine]]
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[[Category: Structural genomic]]
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[[Category: Structural proteomics in europe]]
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Current revision

ISOTYPE SELECTIVITY OF THE HUMAN RETINOIC ACID NUCLEAR RECEPTOR HRAR: THE COMPLEX WITH THE RARGAMMA-SELECTIVE RETINOID SR11254

PDB ID 1fd0

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