5nkx

HRSV M2-1 core domain, P3221 crystal form

spinqualitylabelsall models 5nkx, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nkx is a 2 chain structure with sequence from Human orthopneumovirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.0000868Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q4KRW3_HRSV Publication Abstract from PubMed 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 M2-1. The puzzling mechanism of action of M2-1, 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 M2-1 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. Structure and stability of the Human respiratory syncytial virus M2-1 RNA-binding core domain reveals a compact and cooperative folding unit.,Molina IG, Josts I, Almeida Hernandez Y, Esperante S, Salgueiro M, Garcia Alai MM, de Prat-Gay G, Tidow H Acta Crystallogr F Struct Biol Commun. 2018 Jan 1;74(Pt 1):23-30. doi:, 10.1107/S2053230X17017381. Epub 2017 Dec 15. PMID:29372904 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures M2 protein

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