1k1v

From Proteopedia

(Difference between revisions)

Current revision

Solution Structure of the DNA-Binding Domain of MafG

Structural highlights

1k1v is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAFG_MOUSE Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor. Transcription factor, component of erythroid-specific transcription factor NF-E2. Activates globin gene expression when associated with NF-E2. May be involved in signal transduction of extracellular H(+) (By similarity).^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shavit JA, Motohashi H, Onodera K, Akasaka J, Yamamoto M, Engel JD. Impaired megakaryopoiesis and behavioral defects in mafG-null mutant mice. Genes Dev. 1998 Jul 15;12(14):2164-74. PMID:9679061
↑ Motohashi H, Katsuoka F, Miyoshi C, Uchimura Y, Saitoh H, Francastel C, Engel JD, Yamamoto M. MafG sumoylation is required for active transcriptional repression. Mol Cell Biol. 2006 Jun;26(12):4652-63. PMID:16738329 doi:http://dx.doi.org/10.1128/MCB.02193-05
↑ Kusunoki H, Motohashi H, Katsuoka F, Morohashi A, Yamamoto M, Tanaka T. Solution structure of the DNA-binding domain of MafG. Nat Struct Biol. 2002 Apr;9(4):252-6. PMID:11875518 doi:10.1038/nsb771

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k1v"

@@ Line 19: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1k1v ConSurf].
 <div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
+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<ref>PMID:11875518</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1k1v" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1k1v

From Proteopedia

Current revision

Solution Structure of the DNA-Binding Domain of MafG

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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