1a6y: Difference between revisions
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<StructureSection load='1a6y' size='340' side='right'caption='[[1a6y]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1a6y' size='340' side='right'caption='[[1a6y]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a6y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1a6y]] 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=1A6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A6Y FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5IU:5-IODO-2-DEOXYURIDINE-5-MONOPHOSPHATE'>5IU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1a6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6y OCA], [https://pdbe.org/1a6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a6y RCSB], [https://www.ebi.ac.uk/pdbsum/1a6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a6y ProSAT]</span></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=1a6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6y OCA], [https://pdbe.org/1a6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a6y RCSB], [https://www.ebi.ac.uk/pdbsum/1a6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a6y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/NR1D1_HUMAN NR1D1_HUMAN] Functions as a constitutive transcriptional repressor. In collaboration with SP1, activates GJA1 transcription (By similarity). Possible receptor for triiodothyronine.<ref>PMID:2539258</ref> <ref>PMID:1971514</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: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Khorasanizadeh | [[Category: Khorasanizadeh S]] | ||
[[Category: Rastinejad | [[Category: Rastinejad F]] | ||
[[Category: Zhao | [[Category: Zhao Q]] | ||
Latest revision as of 13:48, 2 August 2023
REVERBA ORPHAN NUCLEAR RECEPTOR/DNA COMPLEXREVERBA ORPHAN NUCLEAR RECEPTOR/DNA COMPLEX
Structural highlights
FunctionNR1D1_HUMAN Functions as a constitutive transcriptional repressor. In collaboration with SP1, activates GJA1 transcription (By similarity). Possible receptor for triiodothyronine.[1] [2] 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 PubMedThe nuclear hormone receptors form the largest known family of transcription factors. The current notion of receptor DNA discrimination, based solely on one major type of hexameric half-site and a highly conserved 66-residue core DNA-binding domain (DBD), does not adequately describe how more than 150 nonsteroid receptors differentiate among response elements. Here, we describe the 2.3 A crystal structure of the DNA-binding region of the orphan receptor RevErb arranged as a tandem homodimer on its optimal response element. The structure reveals the presence of a second major protein-DNA interface adjacent to the classical one involving the half-sites. A sequence comparison of orphan receptors suggests that unique minor-groove interactions involving the receptor hinge regions impart the necessary DNA and dimerization specificity. Structural elements of an orphan nuclear receptor-DNA complex.,Zhao Q, Khorasanizadeh S, Miyoshi Y, Lazar MA, Rastinejad F Mol Cell. 1998 May;1(6):849-61. PMID:9660968[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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