2jw6

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[[Image:2jw6.jpg|left|200px]]
 
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==Solution structure of the DEAF1 MYND domain==
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The line below this paragraph, containing "STRUCTURE_2jw6", creates the "Structure Box" on the page.
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<StructureSection load='2jw6' size='340' side='right'caption='[[2jw6]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2jw6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2fv6 2fv6]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JW6 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_2jw6| PDB=2jw6 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jw6 OCA], [https://pdbe.org/2jw6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jw6 RCSB], [https://www.ebi.ac.uk/pdbsum/2jw6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jw6 ProSAT]</span></td></tr>
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</table>
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'''Solution structure of the DEAF1 MYND domain'''
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== Function ==
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[https://www.uniprot.org/uniprot/DEAF1_HUMAN DEAF1_HUMAN] Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction. When secreted, behaves as an inhibitor of cell proliferation, by arresting cells in the G0 or G1 phase. Required for neural tube closure and skeletal patterning. Regulates epithelial cell proliferation and side-branching in the mammary gland. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Isoform 1 displays greater transcriptional activity than isoform 4. Isoform 4 may inhibit transcriptional activity of isoform 1 by interacting with isoform 1 and retaining it in the cytoplasm.<ref>PMID:11705868</ref> <ref>PMID:19668219</ref> <ref>PMID:10521432</ref> <ref>PMID:11427895</ref> <ref>PMID:18826651</ref>
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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The MYND domain (named after myeloid translocation protein 8, Nervy, and DEAF-1) is a conserved zinc binding domain. It is defined by seven conserved cysteine residues and a single histidine residue that are arranged in a C4-C2HC consensus. MYND domains exist in a large number of proteins that play important roles in development or are associated with cancers and have been shown to mediate protein-protein interactions, mainly in the context of transcriptional regulation. We have determined the three-dimensional structure of the MYND domain from human deformed epidermal autoregulatory factor-1 (DEAF-1). The structure reveals a novel zinc binding fold, in which the C4-C2HC motif forms two sequential zinc binding sites. The first and second zinc binding modules comprise a small beta hairpin and two short alpha helices, respectively. The sequential topology of the two zinc binding sites is distinct from the cross-brace PHD and RING finger folds but has some resemblance to LIM domains. The structure reveals that the MYND domain is a novel member of the treble-clef family of zinc binding domains. The MYND domains of BS69 and BOP bind ligands comprising a PXLXP peptide motif. On the basis of the solution structure of the DEAF-1 MYND domain we calculated a homology model of the MYND domain of the BS69 tumor suppressor. A mutational analysis of the BS69 MYND domain indicates that positively charged residues located on one face of its MYND domain are crucial for the molecular interactions of BS69. Different binding specificities of MYND domains may depend on distinct surface charge distributions.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jw/2jw6_consurf.spt"</scriptWhenChecked>
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2JW6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2fv6 2fv6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JW6 OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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Structure and functional analysis of the MYND domain., Spadaccini R, Perrin H, Bottomley MJ, Ansieau S, Sattler M, J Mol Biol. 2006 Apr 28;358(2):498-508. Epub 2006 Feb 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16527309 16527309]
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</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=2jw6 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Ansieu, S.]]
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[[Category: Ansieu S]]
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[[Category: Bottomley, M.]]
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[[Category: Bottomley M]]
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[[Category: Perrin, H.]]
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[[Category: Perrin H]]
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[[Category: Sattler, M.]]
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[[Category: Sattler M]]
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[[Category: Spadaccini, R.]]
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[[Category: Spadaccini R]]
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[[Category: Alternative splicing]]
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[[Category: Disease mutation]]
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[[Category: Dna-binding]]
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[[Category: Metal-binding]]
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[[Category: Nucleus]]
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[[Category: Phosphorylation]]
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[[Category: Secreted]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Zinc binding domain]]
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[[Category: Zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:20:55 2008''
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Current revision

Solution structure of the DEAF1 MYND domain

PDB ID 2jw6

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