6qu1
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Crystal structure of the KAP1 RBCC domain in complex with the SMARCAD1 CUE1 domain at 3.7 angstrom resolution.== |
| + | <StructureSection load='6qu1' size='340' side='right'caption='[[6qu1]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6qu1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QU1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QU1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></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=6qu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qu1 OCA], [http://pdbe.org/6qu1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qu1 RCSB], [http://www.ebi.ac.uk/pdbsum/6qu1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qu1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/SMRCD_HUMAN SMRCD_HUMAN]] Huriez syndrome;Isolated congenital adermatoglyphia;Absence of fingerprints-congenital milia syndrome. The disease is caused by mutations affecting the gene represented in this entry. Splice site mutations causing aberrant splicing of skin-specific isoform 3 are likely to exert a loss-of-function effect and are involved in ADERM.<ref>PMID:21820097</ref> <ref>PMID:24909267</ref> The disease is caused by mutations affecting the gene represented in this entry. Splice site mutations causing aberrant splicing of skin-specific isoform 3 are likely to exert a loss-of-function effect and are involved in BSNS.<ref>PMID:24664640</ref> <ref>PMID:26932190</ref> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TIF1B_HUMAN TIF1B_HUMAN]] Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6.<ref>PMID:8769649</ref> <ref>PMID:9016654</ref> <ref>PMID:10347202</ref> <ref>PMID:11959841</ref> <ref>PMID:15882967</ref> <ref>PMID:16107876</ref> <ref>PMID:17178852</ref> <ref>PMID:16862143</ref> <ref>PMID:17079232</ref> <ref>PMID:17704056</ref> <ref>PMID:17942393</ref> <ref>PMID:18082607</ref> <ref>PMID:18060868</ref> <ref>PMID:20858735</ref> <ref>PMID:20864041</ref> <ref>PMID:20424263</ref> <ref>PMID:21940674</ref> [[http://www.uniprot.org/uniprot/SMRCD_HUMAN SMRCD_HUMAN]] DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking DSBs. Required for the restoration of heterochromatin organization after replication. Acts at replication sites to facilitate the maintenance of heterochromatin by directing H3 and H4 histones deacetylation, H3 'Lys-9' trimethylation (H3K9me3) and restoration of silencing.<ref>PMID:21549307</ref> <ref>PMID:22960744</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ubiquitylation, the posttranslational linkage of ubiquitin moieties to lysines in target proteins, helps regulate a myriad of biological processes. Ubiquitin, and sometimes ubiquitin-homology domains, are recognized by ubiquitin-binding domains, including CUE domains. CUE domains are thus generally thought to function by mediating interactions with ubiquitylated proteins. The chromatin remodeler, SMARCAD1, interacts with KAP1, a transcriptional corepressor. The SMARCAD1-KAP1 interaction is direct and involves the first SMARCAD1 CUE domain (CUE1) and the RBCC domain of KAP1. Here, we present a structural model of the KAP1 RBCC-SMARCAD1 CUE1 complex based on X-ray crystallography. Remarkably, CUE1, a canonical CUE domain, recognizes a cluster of exposed hydrophobic and surrounding charged/amphipathic residues on KAP1, which are presented in the context of a coiled-coil domain, not in a structure resembling ubiquitin. Together, these data suggest that CUE domains may have a wider function than simply recognizing ubiquitin and the ubiquitin-fold. | ||
| - | + | A Ubiquitin-Binding Domain that Binds a Structural Fold Distinct from that of Ubiquitin.,Lim M, Newman JA, Williams HL, Masino L, Aitkenhead H, Gravard AE, Gileadi O, Svejstrup JQ Structure. 2019 May 28. pii: S0969-2126(19)30165-0. doi:, 10.1016/j.str.2019.05.003. PMID:31204252<ref>PMID:31204252</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 6qu1" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: DNA helicase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Aitkenhead, H]] | [[Category: Aitkenhead, H]] | ||
| - | [[Category: | + | [[Category: Arrowsmith, C H]] |
| - | [[Category: | + | [[Category: Bountra, C]] |
| + | [[Category: Delft, F von]] | ||
[[Category: Edwards, A]] | [[Category: Edwards, A]] | ||
[[Category: Gavard, A]] | [[Category: Gavard, A]] | ||
| - | [[Category: | + | [[Category: Gileadi, O]] |
| + | [[Category: Lim, M]] | ||
| + | [[Category: Newman, J A]] | ||
| + | [[Category: Svejstrup, J Q]] | ||
| + | [[Category: Williams, H L]] | ||
| + | [[Category: Cue domain]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Transcriptional co-repressor]] | ||
| + | [[Category: Trim28]] | ||
| + | [[Category: Ubuiquitin]] | ||
Revision as of 10:51, 17 July 2019
Crystal structure of the KAP1 RBCC domain in complex with the SMARCAD1 CUE1 domain at 3.7 angstrom resolution.
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