5UJN
Representative 2-conformer ensembles of K27-linked Ub2 from RDC data
5UJN の概要
| エントリーDOI | 10.2210/pdb5ujn/pdb |
| 関連するPDBエントリー | 5UJL |
| NMR情報 | BMRB: 30234 |
| 分子名称 | Ubiquitin (1 entity in total) |
| 機能のキーワード | diubiquitin, k27, polyubiquitin chain, signaling protein |
| 由来する生物種 | Homo sapiens (Human) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 17153.66 |
| 構造登録者 | |
| 主引用文献 | Castaneda, C.A.,Dixon, E.K.,Walker, O.,Chaturvedi, A.,Nakasone, M.A.,Curtis, J.E.,Reed, M.R.,Krueger, S.,Cropp, T.A.,Fushman, D. Linkage via K27 Bestows Ubiquitin Chains with Unique Properties among Polyubiquitins. Structure, 24:423-436, 2016 Cited by PubMed Abstract: Polyubiquitination, a critical protein post-translational modification, signals for a diverse set of cellular events via the different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the ɛ-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. We assembled di-ubiquitins (Ub2) comprising every lysine linkage and examined them biochemically and structurally. Of these, K27-Ub2 is unique as it is not cleaved by most deubiquitinases. As this remains the only structurally uncharacterized lysine linkage, we comprehensively examined the structures and dynamics of K27-Ub2 using nuclear magnetic resonance, small-angle neutron scattering, and in silico ensemble modeling. Our structural data provide insights into the functional properties of K27-Ub2, in particular that K27-Ub2 may be specifically recognized by K48-selective receptor UBA2 domain from proteasomal shuttle protein hHR23a. Binding studies and mutagenesis confirmed this prediction, further highlighting structural/recognition versatility of polyubiquitins and the potential power of determining function from elucidation of conformational ensembles. PubMed: 26876099DOI: 10.1016/j.str.2016.01.007 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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