3mln: Difference between revisions
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==DNA binding domain of Early B-cell Factor 1 (Ebf1) bound to DNA (crystal form II)== | |||
<StructureSection load='3mln' size='340' side='right' caption='[[3mln]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3mln]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MLN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MLN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mlo|3mlo]], [[3mlp|3mlp]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ebf1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mln OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mln RCSB], [http://www.ebi.ac.uk/pdbsum/3mln PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Grosschedl, R | [[Category: Grosschedl, R]] | ||
[[Category: Treiber, N | [[Category: Treiber, N]] | ||
[[Category: Treiber, T | [[Category: Treiber, T]] | ||
[[Category: Zocher, G | [[Category: Zocher, G]] | ||
[[Category: Dna]] | [[Category: Dna]] | ||
[[Category: Pseudo-ig-fold]] | [[Category: Pseudo-ig-fold]] | ||
Revision as of 14:58, 18 December 2014
DNA binding domain of Early B-cell Factor 1 (Ebf1) bound to DNA (crystal form II)
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