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Structure of an Ebf1:DNA complex reveals unusual DNA recognition and structural homology with Rel proteins.


ABSTRACT: 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-?B. 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.

SUBMITTER: Treiber N 

PROVIDER: S-EPMC2956205 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature

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Structure of an Ebf1:DNA complex reveals unusual DNA recognition and structural homology with Rel proteins.

Treiber Nora N   Treiber Thomas T   Zocher Georg G   Grosschedl Rudolf R  

Genes & development 20100928 20


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-κB. Ebf1 contacts the DNA with two loop-based modules and  ...[more]

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