Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6QU1

Crystal structure of the KAP1 RBCC domain in complex with the SMARCAD1 CUE1 domain at 3.7 angstrom resolution.

Summary for 6QU1
Entry DOI10.2210/pdb6qu1/pdb
DescriptorTranscription intermediary factor 1-beta,Transcription intermediary factor 1-beta, SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A containing DEAD/H box 1, ZINC ION (3 entities in total)
Functional Keywordstrim28, transcriptional co-repressor, cue domain, ubuiquitin, ligase
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight41590.10
Authors
Newman, J.A.,Aitkenhead, H.,Gavard, A.,Lim, M.,Williams, H.L.,Svejstrup, J.Q.,von Delft, F.,Arrowsmith, C.H.,Edwards, A.,Bountra, C.,Gileadi, O. (deposition date: 2019-02-26, release date: 2019-07-17, Last modification date: 2024-01-24)
Primary citationLim, M.,Newman, J.A.,Williams, H.L.,Masino, L.,Aitkenhead, H.,Gravard, A.E.,Gileadi, O.,Svejstrup, J.Q.
A Ubiquitin-Binding Domain that Binds a Structural Fold Distinct from that of Ubiquitin.
Structure, 2019
Cited by
PubMed Abstract: 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.
PubMed: 31204252
DOI: 10.1016/j.str.2019.05.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.7 Å)
Structure validation

227111

건을2024-11-06부터공개중

PDB statisticsPDBj update infoContact PDBjnumon