1KNZ
Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer
1KNZ の概要
| エントリーDOI | 10.2210/pdb1knz/pdb |
| 分子名称 | 5'-R(*UP*GP*AP*CP*C)-3', Nonstructural RNA-binding Protein 34 (3 entities in total) |
| 機能のキーワード | protein-ssrna complex, viral protein-rna complex, viral protein/rna |
| 由来する生物種 | Simian rotavirus A/SA11 |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 153223.97 |
| 構造登録者 | Deo, R.C.,Groft, C.M.,Rajashankar, K.R.,Burley, S.K. (登録日: 2001-12-19, 公開日: 2002-01-17, 最終更新日: 2024-02-14) |
| 主引用文献 | Deo, R.C.,Groft, C.M.,Rajashankar, K.R.,Burley, S.K. Recognition of the rotavirus mRNA 3' consensus by an asymmetric NSP3 homodimer. Cell(Cambridge,Mass.), 108:71-81, 2002 Cited by PubMed Abstract: Rotaviruses, the cause of life-threatening diarrhea in humans and cattle, utilize a functional homolog of poly(A) binding protein (PABP) known as nonstructural protein 3 (NSP3) for translation of viral mRNAs. NSP3 binds to viral mRNA 3' consensus sequences and circularizes the mRNA via interactions with eIF4G. The X-ray structure of the NSP3 RNA binding domain bound to a rotaviral mRNA 3' end has been determined. NSP3 is a novel, heart-shaped homodimer with a medial RNA binding cleft. The homodimer is asymmetric, and contains two similar N-terminal segments plus two structurally different C-terminal segments that intertwine to create a tunnel enveloping the mRNA 3' end. Biophysical studies demonstrate high affinity binding leading to increased thermal stability and slow dissociation kinetics, consistent with NSP3 function. PubMed: 11792322DOI: 10.1016/S0092-8674(01)00632-8 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.45 Å) |
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