5zfy
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human DUX4 homeodomains bound to A12C DNA mutant== | |
| + | <StructureSection load='5zfy' size='340' side='right' caption='[[5zfy]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5zfy]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZFY 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=5zfy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zfy OCA], [http://pdbe.org/5zfy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zfy RCSB], [http://www.ebi.ac.uk/pdbsum/5zfy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zfy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DU4L4_HUMAN DU4L4_HUMAN]] May be involved in transcriptional regulation. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | DUX4 plays critical role in the molecular pathogenesis of the neuromuscular disorder facioscapulohumeral muscular dystrophy and acute lymphoblastic leukemia in humans. As a master transcription regulator, DUX4 can also bind the promoters and activate the transcription of hundreds ZGA-associated genes. Here we report on the structural and biochemical studies of DUX4 double homeodomains (DUX4-DH), representing the only structures contain both homeodomain 1 (HD1) and homeodomain 2 (HD2). HD1 and HD2 adopt classical homeobox fold; via the helix inserted into the major groove and the N-terminal extended loop inserted into the minor groove, HD1 and HD2 recognize the box1 (5'-TAA-3') and box2 (5'-TGA-3') nucleotides of the consensus sequence, respectively. Among the box1 and box2 linking nucleotides (CCTAA), the two adenine residues are reported to be highly conserved; however, they are not directly recognized by DUX4-DH in the structures. Besides different nucleotides, our ITC analysis indicated that DUX4-DH can also tolerate various changes in the linker length. Our studies not only revealed the basis for target DNA recognition by DUX4, but also advanced our understanding on multiple gene activation by DUX4. | ||
| - | + | Structural basis for multiple gene regulation by human DUX4.,Li Y, Wu B, Liu H, Gao Y, Yang C, Chen X, Zhang J, Chen Y, Gu Y, Li J, Ma J, Gan J Biochem Biophys Res Commun. 2018 Oct 12. pii: S0006-291X(18)32202-2. doi:, 10.1016/j.bbrc.2018.10.056. PMID:30322619<ref>PMID:30322619</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5zfy" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Gan, J H]] | ||
| + | [[Category: Li, Y Y]] | ||
| + | [[Category: Wu, B X]] | ||
| + | [[Category: Dna recognition]] | ||
| + | [[Category: Dux4]] | ||
| + | [[Category: Homeodomain]] | ||
| + | [[Category: Transcription-dna complex]] | ||
Revision as of 06:45, 31 October 2018
Crystal structure of human DUX4 homeodomains bound to A12C DNA mutant
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