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ABSTRACT 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 α-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. Access through your institution Buy or subscribe This is a preview of subscription content, access via your institution ACCESS OPTIONS
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institutional subscriptions * Read our FAQs * Contact customer support SIMILAR CONTENT BEING VIEWED BY OTHERS STRUCTURE OF THE HUMAN SAGA COACTIVATOR COMPLEX Article Open access 22 November
2021 COMPARATIVE STRUCTURAL INSIGHTS AND FUNCTIONAL ANALYSIS FOR THE DISTINCT UNBOUND STATES OF HUMAN AGO PROTEINS Article Open access 19 March 2025 STRUCTURE AND ASSEMBLY OF THE NOT10:11
MODULE OF THE CCR4-NOT COMPLEX Article Open access 17 July 2023 ACCESSION CODES ACCESSIONS GENBANK/EMBL/DDBJ * O42290 * O54790 * O54791 * P34707 * P54841 * P54846 * Q61827 * Q92171 PROTEIN
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for useful discussion, K. Yap for providing a program to calculate interhelical angles and T. O'Connor for critical reading of the manuscript. This work was supported by grants from
JSPS and TARA (T.T.); the Ministry of Education, Science, Sports and Culture of Japan (H.M. and M.Y.); JSPS and CREST (M.Y.); and PROBRAIN (H.M.). AUTHOR INFORMATION AUTHORS AND AFFILIATIONS
* Institute of Basic Medical Science, University of Tsukuba, Tsukuba, 305-8575, Ibaraki, Japan Hideki Kusunoki, Hozumi Motohashi, Fumiki Katsuoka & Masayuki Yamamoto * Center for
Tsukuba Advanced Research Alliance, University of Tsukuba, Tsukuba, 305-8577, Ibaraki, Japan Hideki Kusunoki, Hozumi Motohashi, Masayuki Yamamoto & Toshiyuki Tanaka * Institute of
Applied Biochemistry, University of Tsukuba, Tsukuba, 305-8572, Ibaraki, Japan Akio Morohashi & Toshiyuki Tanaka * Banyu Tsukuba Research Institute, Tsukuba, 300-2611, Ibaraki, Japan
Akio Morohashi Authors * Hideki Kusunoki View author publications You can also search for this author inPubMed Google Scholar * Hozumi Motohashi View author publications You can also search
for this author inPubMed Google Scholar * Fumiki Katsuoka View author publications You can also search for this author inPubMed Google Scholar * Akio Morohashi View author publications You
can also search for this author inPubMed Google Scholar * Masayuki Yamamoto View author publications You can also search for this author inPubMed Google Scholar * Toshiyuki Tanaka View
author publications You can also search for this author inPubMed Google Scholar CORRESPONDING AUTHOR Correspondence to Toshiyuki Tanaka. ETHICS DECLARATIONS COMPETING INTERESTS The authors
declare no competing financial interests. RIGHTS AND PERMISSIONS Reprints and permissions ABOUT THIS ARTICLE CITE THIS ARTICLE Kusunoki, H., Motohashi, H., Katsuoka, F. _et al._ Solution
structure of the DNA-binding domain of MafG. _Nat Struct Mol Biol_ 9, 252–256 (2002). https://doi.org/10.1038/nsb771 Download citation * Received: 02 October 2001 * Accepted: 24 January 2002
* Published: 04 March 2002 * Issue Date: 01 April 2002 * DOI: https://doi.org/10.1038/nsb771 SHARE THIS ARTICLE Anyone you share the following link with will be able to read this content:
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