8cef: Difference between revisions
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==Asymmetric Dimerization in a Transcription Factor Superfamily is Promoted by Allosteric Interactions with DNA== | |||
<StructureSection load='8cef' size='340' side='right'caption='[[8cef]], [[Resolution|resolution]] 2.49Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8cef]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/DNA_molecule DNA molecule] 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=8CEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CEF 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]] 2.486Å</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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8cef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cef OCA], [https://pdbe.org/8cef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cef RCSB], [https://www.ebi.ac.uk/pdbsum/8cef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cef ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Transcription factors, such as nuclear receptors achieve precise transcriptional regulation by means of a tight and reciprocal communication with DNA, where cooperativity gained by receptor dimerization is added to binding site sequence specificity to expand the range of DNA target gene sequences. To unravel the evolutionary steps in the emergence of DNA selection by steroid receptors (SRs) from monomeric to dimeric palindromic binding sites, we carried out crystallographic, biophysical and phylogenetic studies, focusing on the estrogen-related receptors (ERRs, NR3B) that represent closest relatives of SRs. Our results, showing the structure of the ERR DNA-binding domain bound to a palindromic response element (RE), unveil the molecular mechanisms of ERR dimerization which are imprinted in the protein itself with DNA acting as an allosteric driver by allowing the formation of a novel extended asymmetric dimerization region (KR-box). Phylogenetic analyses suggest that this dimerization asymmetry is an ancestral feature necessary for establishing a strong overall dimerization interface, which was progressively modified in other SRs in the course of evolution. | |||
Asymmetric dimerization in a transcription factor superfamily is promoted by allosteric interactions with DNA.,Patel AKM, Vilela P, Shaik TB, McEwen AG, Hazemann I, Brillet K, Ennifar E, Hamiche A, Markov GV, Laudet V, Moras D, Klaholz BP, Billas IML Nucleic Acids Res. 2023 Jul 28:gkad632. doi: 10.1093/nar/gkad632. PMID:37503845<ref>PMID:37503845</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8cef" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: DNA molecule]] | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Billas IML]] | |||
[[Category: Klaholz BP]] | |||
[[Category: McEwen AG]] | |||
[[Category: Moras D]] | |||
[[Category: Patel AKM]] | |||
[[Category: Shaik TB]] | |||
Latest revision as of 08:25, 9 August 2023
Asymmetric Dimerization in a Transcription Factor Superfamily is Promoted by Allosteric Interactions with DNAAsymmetric Dimerization in a Transcription Factor Superfamily is Promoted by Allosteric Interactions with DNA
Structural highlights
Publication Abstract from PubMedTranscription factors, such as nuclear receptors achieve precise transcriptional regulation by means of a tight and reciprocal communication with DNA, where cooperativity gained by receptor dimerization is added to binding site sequence specificity to expand the range of DNA target gene sequences. To unravel the evolutionary steps in the emergence of DNA selection by steroid receptors (SRs) from monomeric to dimeric palindromic binding sites, we carried out crystallographic, biophysical and phylogenetic studies, focusing on the estrogen-related receptors (ERRs, NR3B) that represent closest relatives of SRs. Our results, showing the structure of the ERR DNA-binding domain bound to a palindromic response element (RE), unveil the molecular mechanisms of ERR dimerization which are imprinted in the protein itself with DNA acting as an allosteric driver by allowing the formation of a novel extended asymmetric dimerization region (KR-box). Phylogenetic analyses suggest that this dimerization asymmetry is an ancestral feature necessary for establishing a strong overall dimerization interface, which was progressively modified in other SRs in the course of evolution. Asymmetric dimerization in a transcription factor superfamily is promoted by allosteric interactions with DNA.,Patel AKM, Vilela P, Shaik TB, McEwen AG, Hazemann I, Brillet K, Ennifar E, Hamiche A, Markov GV, Laudet V, Moras D, Klaholz BP, Billas IML Nucleic Acids Res. 2023 Jul 28:gkad632. doi: 10.1093/nar/gkad632. PMID:37503845[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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