3omo: Difference between revisions
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New page: '''Unreleased structure''' The entry 3omo 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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==Fragment-Based Design of novel Estrogen Receptor Ligands== | |||
<StructureSection load='3omo' size='340' side='right'caption='[[3omo]], [[Resolution|resolution]] 2.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3omo]] 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=3OMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OMO 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]] 2.21Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=WV7:2-(TRIFLUOROACETYL)-1,2,3,4-TETRAHYDROISOQUINOLIN-6-OL'>WV7</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=3omo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3omo OCA], [https://pdbe.org/3omo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3omo RCSB], [https://www.ebi.ac.uk/pdbsum/3omo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3omo 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]] | |||
Latest revision as of 13:35, 21 February 2024
Fragment-Based Design of novel Estrogen Receptor LigandsFragment-Based Design of novel Estrogen Receptor Ligands
Structural highlights
FunctionESR2_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 |
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