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| | ==Solution Structure of the DNA-Binding Domain of MafG== | | ==Solution Structure of the DNA-Binding Domain of MafG== |
| - | <StructureSection load='1k1v' size='340' side='right' caption='[[1k1v]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1k1v' size='340' side='right'caption='[[1k1v]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1k1v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K1V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1k1v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K1V FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1v OCA], [http://pdbe.org/1k1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k1v RCSB], [http://www.ebi.ac.uk/pdbsum/1k1v PDBsum]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1v OCA], [https://pdbe.org/1k1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k1v RCSB], [https://www.ebi.ac.uk/pdbsum/1k1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k1v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MAFG_MOUSE 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).<ref>PMID:9679061</ref> <ref>PMID:16738329</ref> | + | [https://www.uniprot.org/uniprot/MAFG_MOUSE 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).<ref>PMID:9679061</ref> <ref>PMID:16738329</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k1/1k1v_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k1/1k1v_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Katsuoka, F]] | + | [[Category: Mus musculus]] |
| - | [[Category: Kusunoki, H]] | + | [[Category: Katsuoka F]] |
| - | [[Category: Morohashi, A]] | + | [[Category: Kusunoki H]] |
| - | [[Category: Motohashi, H]] | + | [[Category: Morohashi A]] |
| - | [[Category: Tanaka, T]] | + | [[Category: Motohashi H]] |
| - | [[Category: Yamamoto, M]] | + | [[Category: Tanaka T]] |
| - | [[Category: Dna binding protein]]
| + | [[Category: Yamamoto M]] |
| - | [[Category: Dna-binding domain]]
| + | |
| - | [[Category: Maf]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
| Structural highlights
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
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