8A1I
Crystal structure of murine Armc8 isoform beta
8A1I の概要
| エントリーDOI | 10.2210/pdb8a1i/pdb |
| 分子名称 | Isoform 2 of Armadillo repeat-containing protein 8, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, CHLORIDE ION, ... (6 entities in total) |
| 機能のキーワード | ctlh complex, armadillo repeats, ubiquitin ligase, protein binding |
| 由来する生物種 | Mus musculus (house mouse) |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 136936.22 |
| 構造登録者 | |
| 主引用文献 | van Gen Hassend, P.M.,Pottikkadavath, A.,Delto, C.,Kuhn, M.,Endres, M.,Schonemann, L.,Schindelin, H. RanBP9 controls the oligomeric state of CTLH complex assemblies. J.Biol.Chem., 299:102869-102869, 2023 Cited by PubMed Abstract: The CTLH (C-terminal to lissencephaly-1 homology motif) complex is a multisubunit RING E3 ligase with poorly defined substrate specificity and flexible subunit composition. Two key subunits, muskelin and Wdr26, specify two alternative CTLH complexes that differ in quaternary structure, thereby allowing the E3 ligase to presumably target different substrates. With the aid of different biophysical and biochemical techniques, we characterized CTLH complex assembly pathways, focusing not only on Wdr26 and muskelin but also on RanBP9, Twa1, and Armc8β subunits, which are critical to establish the scaffold of this E3 ligase. We demonstrate that the ability of muskelin to tetramerize and the assembly of Wdr26 into dimers define mutually exclusive oligomerization modules that compete with nanomolar affinity for RanBP9 binding. The remaining scaffolding subunits, Armc8β and Twa1, strongly interact with each other and with RanBP9, again with nanomolar affinity. Our data demonstrate that RanBP9 organizes subunit assembly and prevents higher order oligomerization of dimeric Wdr26 and the Armc8β-Twa1 heterodimer through its tight binding. Combined, our studies define alternative assembly pathways of the CTLH complex and elucidate the role of RanBP9 in governing differential oligomeric assemblies, thereby advancing our mechanistic understanding of CTLH complex architectures. PubMed: 36621627DOI: 10.1016/j.jbc.2023.102869 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.69 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






