View source for 2ndg


==Solution NMR structures of AF9 yeats domain in complex with histone H3 crotonylation at K18==
<StructureSection load='2ndg' size='340' side='right'caption='[[2ndg]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ndg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NDG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCR:N-6-CROTONYL-L-LYSINE'>KCR</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=2ndg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ndg OCA], [https://pdbe.org/2ndg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ndg RCSB], [https://www.ebi.ac.uk/pdbsum/2ndg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ndg ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/AF9_HUMAN AF9_HUMAN] A chromosomal aberration involving MLLT3 is associated with acute leukemias. Translocation t(9;11)(p22;q23) with KMT2A/MLL1. The result is a rogue activator protein.
== Function ==
[https://www.uniprot.org/uniprot/AF9_HUMAN AF9_HUMAN] Component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA.<ref>PMID:20159561</ref> <ref>PMID:20471948</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histone lysine acylations play an important role in the regulation of gene transcription in chromatin. Unlike histone acetyl-lysine, molecular recognition of a recently identified crotonyl-lysine mark is much less understood. Here, we report that the YEATS domain of AF9 preferentially binds crotonyl-lysine over acetyl-lysine in histone H3. Nuclear magnetic resonance structural analysis reveals that crotonyl-lysine of histone H3 lysine 18 is engulfed deep in an aromatic cage of the YEATS domain where the carbonyl oxygen of crotonyl-lysine forms a hydrogen bond with the backbone amide of protein residue Tyr78. The crotonyl-lysine, through its unique electron-rich double-bond side chain, engages pi-pi aromatic stacking and extended hydrophobic/aromatic interactions with the YEATS domain compared with acetyl-lysine. Our mutational analysis confirmed key protein residues Phe59 and Tyr78 for crotonyl-lysine recognition. Importantly, our findings present a new structural mechanism of protein-protein interactions mediated by histone lysine crotonylation, and show how the cells interpret acyl-lysine marks in different biological contexts.

Structural Insights into Histone Crotonyl-Lysine Recognition by the AF9 YEATS Domain.,Zhang Q, Zeng L, Zhao C, Ju Y, Konuma T, Zhou MM Structure. 2016 Sep 6;24(9):1606-1612. doi: 10.1016/j.str.2016.05.023. Epub 2016 , Aug 18. PMID:27545619<ref>PMID:27545619</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ndg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Zeng L]]
[[Category: Zhou M]]