2F0R
Crystallographic structure of human Tsg101 UEV domain
2F0R の概要
| エントリーDOI | 10.2210/pdb2f0r/pdb |
| 関連するPDBエントリー | 1s1q |
| 分子名称 | Tumor susceptibility gene 101 protein, SULFATE ION (3 entities in total) |
| 機能のキーワード | tsg101, unknown function |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cytoplasm : Q99816 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 36674.45 |
| 構造登録者 | Camara-Artigas, A.,Luque, I.,Palencia, A.,Martinez, J.C.,Mateo, P.L. (登録日: 2005-11-13, 公開日: 2006-03-28, 最終更新日: 2023-08-23) |
| 主引用文献 | Palencia, A.,Martinez, J.C.,Mateo, P.L.,Luque, I.,Camara-Artigas, A. Structure of human TSG101 UEV domain. Acta Crystallogr.,Sect.D, 62:458-464, 2006 Cited by PubMed Abstract: The UEV domain of the TSG101 protein functions in the vacuolar protein-sorting pathway and in the budding process of HIV-1 and other retroviruses by recognizing ubiquitin in proteins tagged for degradation and short sequences in viral proteins containing an essential and well conserved PTAP motif, respectively. A deep understanding of these interactions is key to the rational design of much-needed novel antivirals. Here, the crystal structure of the TSG101 UEV domain (TSG101-UEV) is presented. TSG101-UEV was crystallized in the presence of PEG 4000 and ammonium sulfate. Under these conditions, crystals were obtained in space group R3, with unit-cell parameters a = b = 97.9, c = 110.6 A, alpha = beta = 90, gamma = 120 degrees . Phases were solved by molecular replacement and the crystal structure of TSG101-UEV was refined to an R factor of 18.8% at 2.2 A resolution. A comparison between the crystal structure and previously reported NMR structures has revealed significant differences in the conformation of one of the loops implicated in ubiquitin recognition. Also, the resulting structure has provided information about the presence of water molecules at the binding interface that could be of relevance for peptide recognition. PubMed: 16552148DOI: 10.1107/S0907444906005221 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.26 Å) |
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