1k1v
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(New page: 200px<br /><applet load="1k1v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k1v" /> '''Solution Structure of the DNA-Binding Domain...)
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Revision as of 16:39, 20 November 2007
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Solution Structure of the DNA-Binding Domain of MafG
Overview
The Maf family proteins, which constitute a subgroup of basic, region-leucine zipper (bZIP) proteins, function as transcriptional, regulators of cellular differentiation. Together with the basic region, the Maf extended homology region (EHR), conserved only within the Maf, family, defines the DNA binding specific to Mafs. Here we present the, first NMR-derived structure of the DNA-binding domain (residues 1-76) of, MafG, which contains the EHR and the basic region. The structure consists, of three alpha-helices and resembles the fold of the DNA-binding domain of, Skn-1, a developmental transcription factor of Caenorhabditis elegans. The, structural similarity between MafG and Skn-1 enables us to propose a, possible mechanism by which Maf family proteins recognize their consensus, DNA sequences.
About this Structure
1K1V is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Solution structure of the DNA-binding domain of MafG., Kusunoki H, Motohashi H, Katsuoka F, Morohashi A, Yamamoto M, Tanaka T, Nat Struct Biol. 2002 Apr;9(4):252-6. PMID:11875518
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