3KWI
X-ray structure of NS1 effector domain W187Y mutant
3KWI の概要
| エントリーDOI | 10.2210/pdb3kwi/pdb |
| 関連するPDBエントリー | 3EE8 3EE9 3KWG |
| 分子名称 | Non-structural protein 1 (2 entities in total) |
| 機能のキーワード | influenza, ns1, effector domain, alternative splicing, host cytoplasm, host nucleus, host-virus interaction, interferon antiviral system evasion, rna-binding, suppressor of rna silencing, viral protein |
| 由来する生物種 | Influenza A virus |
| 細胞内の位置 | Host nucleus: P03495 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 32028.85 |
| 構造登録者 | |
| 主引用文献 | Xia, S.,Robertus, J.D. X-ray structures of NS1 effector domain mutants. Arch.Biochem.Biophys., 494:198-204, 2010 Cited by PubMed Abstract: The influenza A virus nonstructural protein NS1 is a multifunctional dimeric protein that acts as a potent inhibitor of the host cellular antiviral state. The C-terminal effector domain of NS1 binds host proteins, including CPSF30, and is a target for the development of new antiviral drugs. Here we present crystallographic structures of two mutant effector domains, W187Y and W187A, of influenza A/Udorn/72 virus. Unlike wild-type, the mutants behave exclusively as monomers in solution based on gel filtration data and light scattering. The W187Y mutant is able to bind CPSF30 with a binding affinity close to the wild-type protein; that is, it retains a receptor site for aromatic ligands nearly identical to the wild-type. Therefore, this monomeric mutant protein could serve as a drug target for a high throughput inhibitor screening assays, since its binding pocket is unoccupied in solution and potentially more accessible to small molecule ligands. PubMed: 19995550DOI: 10.1016/j.abb.2009.12.008 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.21 Å) |
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