4dma: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:4dma.png|left|200px]]


<!--
==Crystal structure of ERa LBD in complex with RU100132==
The line below this paragraph, containing "STRUCTURE_4dma", creates the "Structure Box" on the page.
<StructureSection load='4dma' size='340' side='right'caption='[[4dma]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[4dma]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DMA FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0L8:2-BROMO-6-(FURAN-3-YL)-4-(HYDROXYMETHYL)BIPHENYL-4-OL'>0L8</scene></td></tr>
{{STRUCTURE_4dma|  PDB=4dma  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dma OCA], [https://pdbe.org/4dma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dma RCSB], [https://www.ebi.ac.uk/pdbsum/4dma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dma ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ESR1_HUMAN ESR1_HUMAN] Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Isoform 3 is involved in activation of NOS3 and endothelial nitric oxide production. Isoforms lacking one or several functional domains are thought to modulate transcriptional activity by competitive ligand or DNA binding and/or heterodimerization with the full length receptor. Isoform 3 can bind to ERE and inhibit isoform 1.<ref>PMID:7651415</ref> <ref>PMID:10970861</ref> <ref>PMID:9328340</ref> <ref>PMID:10681512</ref> <ref>PMID:10816575</ref> <ref>PMID:11477071</ref> <ref>PMID:11682626</ref> <ref>PMID:15078875</ref> <ref>PMID:16043358</ref> <ref>PMID:15891768</ref> <ref>PMID:16684779</ref> <ref>PMID:18247370</ref> <ref>PMID:17932106</ref> <ref>PMID:19350539</ref> <ref>PMID:20705611</ref> <ref>PMID:21937726</ref> <ref>PMID:21330404</ref> <ref>PMID:22083956</ref>  


===Crystal structure of ERa LBD in complex with RU100132===
==See Also==
 
*[[Estrogen receptor 3D structures|Estrogen receptor 3D structures]]
 
== References ==
<!--
<references/>
The line below this paragraph, {{ABSTRACT_PUBMED_22355136}}, adds the Publication Abstract to the page
__TOC__
(as it appears on PubMed at http://www.pubmed.gov), where 22355136 is the PubMed ID number.
</StructureSection>
-->
{{ABSTRACT_PUBMED_22355136}}
 
==About this Structure==
[[4dma]] is a 4 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=4DMA OCA].
 
==Reference==
<ref group="xtra">PMID:022355136</ref><references group="xtra"/>
[[Category: Histone acetyltransferase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Bourguet, W.]]
[[Category: Large Structures]]
[[Category: Brelivet, Y.]]
[[Category: Mus musculus]]
[[Category: Cura, V.]]
[[Category: Bourguet W]]
[[Category: Eiler, S.]]
[[Category: Brelivet Y]]
[[Category: Moras, D.]]
[[Category: Cura V]]
[[Category: Osz, J.]]
[[Category: Eiler S]]
[[Category: Peluso-Iltis, C.]]
[[Category: Moras D]]
[[Category: Rochel, N.]]
[[Category: Osz J]]
[[Category: Ruff, M.]]
[[Category: Peluso-Iltis C]]
[[Category: Alpha helical sandwich]]
[[Category: Rochel N]]
[[Category: Er]]
[[Category: Ruff M]]
[[Category: Estradiol]]
[[Category: Estrogen receptor]]
[[Category: Nuclear receptor]]
[[Category: Transcription]]
[[Category: Transcription factor]]
[[Category: Transcription-protein binding-agonist complex]]