3d90
From Proteopedia
(Difference between revisions)
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==Crystal structure of the human progesterone receptor ligand-binding domain bound to levonorgestrel== | ==Crystal structure of the human progesterone receptor ligand-binding domain bound to levonorgestrel== | ||
- | <StructureSection load='3d90' size='340' side='right' caption='[[3d90]], [[Resolution|resolution]] 2.26Å' scene=''> | + | <StructureSection load='3d90' size='340' side='right'caption='[[3d90]], [[Resolution|resolution]] 2.26Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3d90]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3d90]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D90 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D90 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NOG:13-BETA-ETHYL-17-ALPHA-ETHYNYL-17-BETA-HYDROXYGON-4-EN-3-ONE'>NOG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NOG:13-BETA-ETHYL-17-ALPHA-ETHYNYL-17-BETA-HYDROXYGON-4-EN-3-ONE'>NOG</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PGR, NR3C3 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PGR, NR3C3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d90 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d90 OCA], [https://pdbe.org/3d90 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d90 RCSB], [https://www.ebi.ac.uk/pdbsum/3d90 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d90 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/PRGR_HUMAN PRGR_HUMAN]] The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor isoform B (PRB) is involved activation of c-SRC/MAPK signaling on hormone stimulation.<ref>PMID:15572662</ref> <ref>PMID:15798179</ref> <ref>PMID:17020914</ref> <ref>PMID:17347654</ref> <ref>PMID:17717077</ref> <ref>PMID:17173941</ref> <ref>PMID:18202149</ref> Isoform A is inactive in stimulating c-Src/MAPK signaling on hormone stimulation.<ref>PMID:15572662</ref> <ref>PMID:15798179</ref> <ref>PMID:17020914</ref> <ref>PMID:17347654</ref> <ref>PMID:17717077</ref> <ref>PMID:17173941</ref> <ref>PMID:18202149</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Fagart, J]] | [[Category: Fagart, J]] | ||
[[Category: Gainer, E]] | [[Category: Gainer, E]] |
Revision as of 07:57, 2 February 2022
Crystal structure of the human progesterone receptor ligand-binding domain bound to levonorgestrel
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Categories: Human | Large Structures | Fagart, J | Gainer, E | Petit-Topin, I | Rafestin-Oblin, M E | Turque, N | Ulman, A | Alternative splicing | Contraception | Dna-binding | Lipid-binding | Metal-binding | Nuclear receptor | Nucleus | Phosphoprotein | Polymorphism | Progesterone receptor | Receptor | Steroid receptor | Steroid-binding | Transcription | Transcription factor | Transcription regulation | Women health | Zinc | Zinc-finger