3mln

DNA binding domain of Early B-cell Factor 1 (Ebf1) bound to DNA (crystal form II)

spinqualitylabelsall models 3mln, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3mln is a 5 chain structure with sequence from Mus musculus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function COE1_MOUSE Transcriptional activator which recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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