3mlo
From Proteopedia
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- | [[ | + | ==DNA binding domain of Early B-cell Factor 1 (Ebf1) bound to DNA (Crystal form I)== |
+ | <StructureSection load='3mlo' size='340' side='right' caption='[[3mlo]], [[Resolution|resolution]] 3.01Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3mlo]] is a 4 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=3MLO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MLO FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mln|3mln]], [[3mlp|3mlp]]</td></tr> | ||
+ | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mlo RCSB], [http://www.ebi.ac.uk/pdbsum/3mlo 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> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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- | == | + | |
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Grosschedl, R.]] | [[Category: Grosschedl, R.]] |
Revision as of 10:30, 28 May 2014
DNA binding domain of Early B-cell Factor 1 (Ebf1) bound to DNA (Crystal form I)
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