3SDM
Structure of oligomeric kinase/RNase Ire1 in complex with an oligonucleotide
3SDM の概要
| エントリーDOI | 10.2210/pdb3sdm/pdb |
| 関連するPDBエントリー | 3fbv 3sdj |
| 分子名称 | Serine/threonine-protein kinase/endoribonuclease IRE1 (1 entity in total) |
| 機能のキーワード | kinase, rnase, ribonuclease, hac1, xbp1, splicing, rna, upr, unfolded protein response, oligomer, complex, oligonucleotide, transferase, hydrolase |
| 由来する生物種 | Saccharomyces cerevisiae (Baker's yeast) |
| タンパク質・核酸の鎖数 | 7 |
| 化学式量合計 | 363183.74 |
| 構造登録者 | Korennykh, A.,Korostelev, A.,Egea, P.,Finer-Moore, J.,Zhang, C.,Stroud, R.,Shokat, K.,Walter, P. (登録日: 2011-06-09, 公開日: 2011-07-13, 最終更新日: 2024-11-20) |
| 主引用文献 | Korennykh, A.V.,Egea, P.F.,Korostelev, A.A.,Finer-Moore, J.,Stroud, R.M.,Zhang, C.,Shokat, K.M.,Walter, P. Cofactor-mediated conformational control in the bifunctional kinase/RNase Ire1. Bmc Biol., 9:48-48, 2011 Cited by PubMed Abstract: Ire1 is a signal transduction protein in the endoplasmic reticulum (ER) membrane that serves to adjust the protein-folding capacity of the ER according to the needs of the cell. Ire1 signals, in a transcriptional program, the unfolded protein response (UPR) via the coordinated action of its protein kinase and RNase domains. In this study, we investigated how the binding of cofactors to the kinase domain of Ire1 modulates its RNase activity. PubMed: 21729334DOI: 10.1186/1741-7007-9-48 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (6.6 Å) |
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