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4aa6

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<StructureSection load='4aa6' size='340' side='right'caption='[[4aa6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='4aa6' size='340' side='right'caption='[[4aa6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4aa6]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AA6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4aa6]] is a 8 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=4AA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AA6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yat|2yat]], [[2yja|2yja]], [[1xp1|1xp1]], [[1qkt|1qkt]], [[1r5k|1r5k]], [[1zky|1zky]], [[2bj4|2bj4]], [[1hcp|1hcp]], [[1akf|1akf]], [[1hcq|1hcq]], [[1a52|1a52]], [[1qku|1qku]], [[1xp6|1xp6]], [[1g50|1g50]], [[1pcg|1pcg]], [[2b1v|2b1v]], [[2jf9|2jf9]], [[1uom|1uom]], [[1yim|1yim]], [[2ayr|2ayr]], [[1yin|1yin]], [[3ert|3ert]], [[1err|1err]], [[1x7r|1x7r]], [[3erd|3erd]], [[1l2i|1l2i]], [[2fai|2fai]], [[1xp9|1xp9]], [[1gwr|1gwr]], [[2jfa|2jfa]], [[1sj0|1sj0]], [[1gwq|1gwq]], [[1xpc|1xpc]], [[1x7e|1x7e]], [[1xqc|1xqc]], [[1ere|1ere]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2yat|2yat]], [[2yja|2yja]], [[1xp1|1xp1]], [[1qkt|1qkt]], [[1r5k|1r5k]], [[1zky|1zky]], [[2bj4|2bj4]], [[1hcp|1hcp]], [[1akf|1akf]], [[1hcq|1hcq]], [[1a52|1a52]], [[1qku|1qku]], [[1xp6|1xp6]], [[1g50|1g50]], [[1pcg|1pcg]], [[2b1v|2b1v]], [[2jf9|2jf9]], [[1uom|1uom]], [[1yim|1yim]], [[2ayr|2ayr]], [[1yin|1yin]], [[3ert|3ert]], [[1err|1err]], [[1x7r|1x7r]], [[3erd|3erd]], [[1l2i|1l2i]], [[2fai|2fai]], [[1xp9|1xp9]], [[1gwr|1gwr]], [[2jfa|2jfa]], [[1sj0|1sj0]], [[1gwq|1gwq]], [[1xpc|1xpc]], [[1x7e|1x7e]], [[1xqc|1xqc]], [[1ere|1ere]]</div></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4aa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aa6 OCA], [http://pdbe.org/4aa6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4aa6 RCSB], [http://www.ebi.ac.uk/pdbsum/4aa6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4aa6 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4aa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aa6 OCA], [https://pdbe.org/4aa6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aa6 RCSB], [https://www.ebi.ac.uk/pdbsum/4aa6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aa6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[[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>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 07:55, 18 August 2022

The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation

PDB ID 4aa6

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