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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[[Image:1k1v.gif|left|200px]]<br /><applet load="1k1v" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Solution Structure of the DNA-Binding Domain of MafG'''<br />
'''Solution Structure of the DNA-Binding Domain of MafG'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1K1V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K1V OCA].
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1K1V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1K1V OCA].
==Reference==
==Reference==
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[[Category: transcription factor]]
[[Category: transcription factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:46:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:13 2008''

Revision as of 11:29, 21 February 2008


1k1v

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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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