1TH0
Structure of human Senp2
1TH0 の概要
エントリーDOI | 10.2210/pdb1th0/pdb |
関連するPDBエントリー | 1TGZ |
分子名称 | Sentrin-specific protease 2 (2 entities in total) |
機能のキーワード | sumo; axam; senp; ulp; protease, cell cycle, hydrolase |
由来する生物種 | Homo sapiens (human) |
細胞内の位置 | Nucleus, nuclear pore complex: Q9HC62 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 53574.17 |
構造登録者 | |
主引用文献 | Reverter, D.,Lima, C.D. A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex Structure, 12:1519-1531, 2004 Cited by PubMed Abstract: Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear metabolism and cell cycle progression in yeast. X-ray structures of the human Senp2 catalytic protease domain and of a covalent thiohemiacetal transition-state complex obtained between the Senp2 catalytic domain and SUMO-1 revealed details of the respective protease and substrate surfaces utilized in interactions between these two proteins. Comparative biochemical and structural analysis between Senp2 and the yeast SUMO protease Ulp1 revealed differential abilities to process SUMO-1, SUMO-2, and SUMO-3 in maturation and deconjugation reactions. Further biochemical characterization of the three SUMO isoforms into which an additional Gly-Gly di-peptide was inserted, or whereby the respective SUMO tails from the three isoforms were swapped, suggests a strict dependence for SUMO isopeptidase activity on residues C-terminal to the conserved Gly-Gly motif and preferred cleavage site for SUMO proteases. PubMed: 15296745DOI: 10.1016/j.str.2004.05.023 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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