3omp
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3omp is ON HOLD Authors: Moecklinghoff, S., van Otterlo, W.A., Rose, R., Fuchs, S., Dominguez Seoane, M., Waldmann, H., Ottmann, C., Brunsveld, L. ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Fragment-Based Design of novel Estrogen Receptor Ligands== | |
| + | <StructureSection load='3omp' size='340' side='right'caption='[[3omp]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3omp]] 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=3OMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OMP FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=W14:2-(TRIFLUOROACETYL)-1,2,3,4-TETRAHYDROISOQUINOLIN-7-OL'>W14</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=3omp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3omp OCA], [https://pdbe.org/3omp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3omp RCSB], [https://www.ebi.ac.uk/pdbsum/3omp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3omp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ESR2_HUMAN ESR2_HUMAN] Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Isoform beta-cx lacks ligand binding ability and has no or only very low ere binding activity resulting in the loss of ligand-dependent transactivation ability. DNA-binding by ESR1 and ESR2 is rapidly lost at 37 degrees Celsius in the absence of ligand while in the presence of 17 beta-estradiol and 4-hydroxy-tamoxifen loss in DNA-binding at elevated temperature is more gradual. | ||
| - | + | ==See Also== | |
| - | + | *[[Estrogen receptor 3D structures|Estrogen receptor 3D structures]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Homo sapiens]] | |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Brunsveld L]] | ||
| + | [[Category: Dominguez Seoane M]] | ||
| + | [[Category: Fuchs S]] | ||
| + | [[Category: Moecklinghoff S]] | ||
| + | [[Category: Ottmann C]] | ||
| + | [[Category: Rose R]] | ||
| + | [[Category: Waldmann H]] | ||
| + | [[Category: Van Otterlo WA]] | ||
Current revision
Fragment-Based Design of novel Estrogen Receptor Ligands
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