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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7toa]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=7TOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TOA FirstGlance]. <br> | <table><tr><td colspan='2'>[[7toa]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=7TOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TOA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.41Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7toa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7toa OCA], [https://pdbe.org/7toa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7toa RCSB], [https://www.ebi.ac.uk/pdbsum/7toa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7toa ProSAT]</span></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=7toa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7toa OCA], [https://pdbe.org/7toa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7toa RCSB], [https://www.ebi.ac.uk/pdbsum/7toa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7toa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | |||
Bromodomains (BDs) regulate gene expression by recognizing protein motifs containing acetyllysine. Although originally characterized as histone-binding proteins, it has since become clear that these domains interact with other acetylated proteins, perhaps most prominently transcription factors. The likely transient nature and low stoichiometry of such modifications, however, has made it challenging to fully define the interactome of any given BD. To begin to address this knowledge gap in an unbiased manner, we carried out mRNA display screens against a BD-the N-terminal BD of BRD3-using peptide libraries that contained either one or two acetyllysine residues. We discovered peptides with very strong consensus sequences and with affinities that are significantly higher than typical BD-peptide interactions. X-ray crystal structures also revealed modes of binding that have not been seen with natural ligands. Intriguingly, however, our sequences are not found in the human proteome, perhaps suggesting that strong binders to BDs might have been selected against during evolution. | |||
mRNA display reveals a class of high-affinity bromodomain-binding motifs that are not found in the human proteome.,Low JKK, Patel K, Jones N, Solomon P, Norman A, Maxwell JWC, Pachl P, Matthews JM, Payne RJ, Passioura T, Suga H, Walport LJ, Mackay JP J Biol Chem. 2023 Dec;299(12):105482. doi: 10.1016/j.jbc.2023.105482. Epub 2023 , Nov 20. PMID:37992806<ref>PMID:37992806</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7toa" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 12:13, 17 October 2024
BRD3-BD1 in complex with RaPID linear peptide 3xAcK.1 (triAcK.1)BRD3-BD1 in complex with RaPID linear peptide 3xAcK.1 (triAcK.1)
Structural highlights
Publication Abstract from PubMedBromodomains (BDs) regulate gene expression by recognizing protein motifs containing acetyllysine. Although originally characterized as histone-binding proteins, it has since become clear that these domains interact with other acetylated proteins, perhaps most prominently transcription factors. The likely transient nature and low stoichiometry of such modifications, however, has made it challenging to fully define the interactome of any given BD. To begin to address this knowledge gap in an unbiased manner, we carried out mRNA display screens against a BD-the N-terminal BD of BRD3-using peptide libraries that contained either one or two acetyllysine residues. We discovered peptides with very strong consensus sequences and with affinities that are significantly higher than typical BD-peptide interactions. X-ray crystal structures also revealed modes of binding that have not been seen with natural ligands. Intriguingly, however, our sequences are not found in the human proteome, perhaps suggesting that strong binders to BDs might have been selected against during evolution. mRNA display reveals a class of high-affinity bromodomain-binding motifs that are not found in the human proteome.,Low JKK, Patel K, Jones N, Solomon P, Norman A, Maxwell JWC, Pachl P, Matthews JM, Payne RJ, Passioura T, Suga H, Walport LJ, Mackay JP J Biol Chem. 2023 Dec;299(12):105482. doi: 10.1016/j.jbc.2023.105482. Epub 2023 , Nov 20. PMID:37992806[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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