View source for 3mlp


==Early B-cell Factor 1 (Ebf1) bound to DNA==
<StructureSection load='3mlp' size='340' side='right'caption='[[3mlp]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3mlp]] is a 8 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=3MLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLP 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]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <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=3mlp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlp OCA], [https://pdbe.org/3mlp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlp RCSB], [https://www.ebi.ac.uk/pdbsum/3mlp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COE1_MOUSE COE1_MOUSE] Transcriptional activator which recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'.<ref>PMID:20876732</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Early B-cell factor 1 (Ebf1) is a key transcriptional determinant of B-lymphocyte differentiation whose DNA-binding domain has no sequence similarity to other transcription factor families. Here we report the crystal structure of an Ebf1 dimer bound to its palindromic recognition site. The DNA-binding domain adopts a pseudoimmunoglobulin-like fold with novel topology, but is structurally similar to the Rel homology domains of NFAT and NF-kappaB. Ebf1 contacts the DNA with two loop-based modules and a unique Zn coordination motif whereby each Ebf1 monomer interacts with both palindromic half-sites. This unusual mode of DNA recognition generates an extended contact area that may be crucial for the function of Ebf1 in chromatin.

Structure of an Ebf1:DNA complex reveals unusual DNA recognition and structural homology with Rel proteins.,Treiber N, Treiber T, Zocher G, Grosschedl R Genes Dev. 2010 Oct 15;24(20):2270-5. Epub 2010 Sep 28. PMID:20876732<ref>PMID:20876732</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3mlp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Synthetic construct]]
[[Category: Grosschedl R]]
[[Category: Treiber N]]
[[Category: Treiber T]]
[[Category: Zocher G]]