1Q0V
Solution Structure of Tandem UIMs of Vps27
1Q0V の概要
| エントリーDOI | 10.2210/pdb1q0v/pdb |
| 関連するPDBエントリー | 1O06 |
| 分子名称 | hydrophilic protein; has cysteine rich putative zinc finger essential for function; Vps27p (1 entity in total) |
| 機能のキーワード | stable, non-interacting alpha-helices, transport binding |
| 由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
| 細胞内の位置 | Endosome membrane; Peripheral membrane protein; Cytoplasmic side: P40343 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 9370.26 |
| 構造登録者 | Swanson, K.A.,Kang, R.S.,Stamenova, S.D.,Hicke, L.,Radhakrishnan, I. (登録日: 2003-07-17, 公開日: 2003-12-23, 最終更新日: 2024-05-22) |
| 主引用文献 | Swanson, K.A.,Kang, R.S.,Stamenova, S.D.,Hicke, L.,Radhakrishnan, I. Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation. Embo J., 22:4597-4606, 2003 Cited by PubMed Abstract: Monoubiquitylation is a well-characterized signal for the internalization and sorting of integral membrane proteins to distinct cellular organelles. Recognition and transmission of monoubiquitin signals is mediated by a variety of ubiquitin-binding motifs such as UIM, UBA, UEV, VHS and CUE in endocytic proteins. The yeast Vps27 protein requires two UIMs for efficient interactions with ubiquitin and for sorting cargo into multivesicular bodies. Here we show that the individual UIMs of Vps27 exist as autonomously folded alpha-helices that bind ubiquitin independently, non-cooperatively and with modest affinity. The Vps27 N-terminal UIM engages the Leu8-Ile44-Val70 hydrophobic patch of ubiquitin through a helical surface conserved in UIMs of diverse proteins, including that of the S5a proteasomal regulatory subunit. The Leu8-Ile44-Val70 ubiquitin surface is also the site of interaction for CUE and UBA domains in endocytic proteins, consistent with the view that ubiquitin-binding endocytic proteins act serially on the same monoubiquitylated cargo during transport from cell surface to the lysosome. PubMed: 12970172DOI: 10.1093/emboj/cdg471 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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