5NKX
HRSV M2-1 core domain, P3221 crystal form
5NKX の概要
| エントリーDOI | 10.2210/pdb5nkx/pdb |
| 分子名称 | M2-1 (2 entities in total) |
| 機能のキーワード | viral protein |
| 由来する生物種 | Human respiratory syncytial virus |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 25361.20 |
| 構造登録者 | Almeida Hernandez, Y.,Josts, I.,Molina, I.G.,de Pray-Gay, G.,Tidow, H. (登録日: 2017-04-03, 公開日: 2018-01-03, 最終更新日: 2024-01-17) |
| 主引用文献 | Molina, I.G.,Josts, I.,Almeida Hernandez, Y.,Esperante, S.,Salgueiro, M.,Garcia Alai, M.M.,de Prat-Gay, G.,Tidow, H. Structure and stability of the Human respiratory syncytial virus M2-1RNA-binding core domain reveals a compact and cooperative folding unit. Acta Crystallogr F Struct Biol Commun, 74:23-30, 2018 Cited by PubMed Abstract: Human syncytial respiratory virus is a nonsegmented negative-strand RNA virus with serious implications for respiratory disease in infants, and has recently been reclassified into a new family, Pneumoviridae. One of the main reasons for this classification is the unique presence of a transcriptional antiterminator, called M. The puzzling mechanism of action of M, which is a rarity among antiterminators in viruses and is part of the RNA polymerase complex, relies on dissecting the structure and function of this multidomain tetramer. The RNA-binding activity is located in a monomeric globular `core' domain, a high-resolution crystal structure of which is now presented. The structure reveals a compact domain which is superimposable on the full-length M tetramer, with additional electron density for the C-terminal tail that was not observed in the previous models. Moreover, its folding stability was determined through chemical denaturation, which shows that the secondary and tertiary structure unfold concomitantly, which is indicative of a two-state equilibrium. These results constitute a further step in the understanding of this unique RNA-binding domain, for which there is no sequence or structural counterpart outside this virus family, in addition to its implications in transcription regulation and its likeliness as an antiviral target. PubMed: 29372904DOI: 10.1107/S2053230X17017381 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.00008687185 Å) |
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