View source for 2lkm


==Structural Basis for Molecular Interactions Involving MRG Domains: Implications in Chromatin Biology==
<StructureSection load='2lkm' size='340' side='right'caption='[[2lkm]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lkm]] 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=2LKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LKM 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lkm OCA], [https://pdbe.org/2lkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lkm RCSB], [https://www.ebi.ac.uk/pdbsum/2lkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lkm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHF12_HUMAN PHF12_HUMAN] Acts as a transcriptional repressor. Involved in recruitment of functional SIN3A complexes to DNA. Represses transcription at least in part through the activity of an associated histone deacetylase (HDAC). May also repress transcription in a SIN3A-independent manner through recruitment of functional AES complexes to DNA.<ref>PMID:11390640</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
MRG15 is a member of the mortality family of transcription factors that targets a wide variety of multiprotein complexes involved in transcription regulation, DNA repair, and alternative splicing to chromatin. The structure of the apo-MRG15 MRG domain implicated in interactions with diverse proteins has been described, but not in complex with any of its targets. Here, we structurally and functionally characterize the interaction between MRG15 and Pf1, two constitutively associated subunits of the histone deacetylase-associated Rpd3S/Sin3S corepressor complex. The MRG domain adopts a structure reminiscent of the apo state, whereas the Pf1 MRG-binding domain engages two discrete hydrophobic surfaces on the MRG domain via a bipartite motif comprising an alpha-helix and a segment in an extended conformation, both of which are critical for high-affinity interactions. Multiple MRG15 interactors share an FxLP motif in the extended segment, but equivalent sequence/helical motifs are not readily evident, implying potential diversity in MRG-recognition mechanisms.

Structural basis for molecular interactions involving MRG domains: implications in chromatin biology.,Xie T, Graveline R, Kumar GS, Zhang Y, Krishnan A, David G, Radhakrishnan I Structure. 2012 Jan 11;20(1):151-60. PMID:22244764<ref>PMID:22244764</ref>

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