6dat: Difference between revisions
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<StructureSection load='6dat' size='340' side='right'caption='[[6dat]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='6dat' size='340' side='right'caption='[[6dat]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6dat]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6dat]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DAT FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3500264Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PF5:2,3,4,5,6-PENTAFLUORO-L-PHENYLALANINE'>PF5</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6dat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dat OCA], [https://pdbe.org/6dat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dat RCSB], [https://www.ebi.ac.uk/pdbsum/6dat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dat ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ETS1_MOUSE ETS1_MOUSE] Transcription factor. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6dat" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6dat" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ets1|Ets1]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Graves | [[Category: Synthetic construct]] | ||
[[Category: Lin | [[Category: Graves BJ]] | ||
[[Category: McIntosh | [[Category: Lin CS]] | ||
[[Category: Murphy | [[Category: McIntosh LP]] | ||
[[Category: Okon | [[Category: Murphy MEP]] | ||
[[Category: Perez-Borrajero | [[Category: Okon M]] | ||
[[Category: Scheu | [[Category: Perez-Borrajero C]] | ||
[[Category: Scheu K]] | |||
Latest revision as of 18:21, 4 October 2023
ETS1 in complex with synthetic SRR mimicETS1 in complex with synthetic SRR mimic
Structural highlights
FunctionETS1_MOUSE Transcription factor. Publication Abstract from PubMedThe eukaryotic transcription factor ETS1 is regulated by an intrinsically disordered serine-rich region (SRR) that transiently associates with the adjacent ETS domain to inhibit DNA binding. In this study, we further elucidated the physicochemical basis for ETS1 autoinhibition by characterizing the interaction of its ETS domain with a series of synthetic peptides corresponding to the SRR. Binding is driven by the hydrophobic effect and enhanced electrostatically by phosphorylation of serines adjacent to aromatic residues in the amphipathic SRR. Structural characterization of the dynamic peptide/protein complex by NMR spectroscopy and X-ray crystallography revealed multiple modes of binding that lead to autoinhibition by synergistically blocking the DNA-binding interface of the ETS domain and stabilizing an appended helical inhibitory module against allosterically induced unfolding. Consistent with these conclusions, the SRR peptide does not interact with DNA-bound ETS1. In addition, we found that the ETS1 SRR phosphopeptide binds to distantly-related PU.1 in vitro, indicating autoinhibition exploits features of the ETS domain that are conserved across this family of transcription factors. The Biophysical Basis for Phosphorylation-Enhanced DNA-Binding Autoinhibition of the ETS1 Transcription Factor.,Perez-Borrajero C, Lin CS, Okon M, Scheu K, Graves BJ, Murphy MEP, McIntosh LP J Mol Biol. 2018 Dec 28. pii: S0022-2836(18)31286-5. doi:, 10.1016/j.jmb.2018.12.011. PMID:30597162[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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