4v5v

Structure of respiratory syncytial virus nucleocapsid protein, P1 crystal form

spinqualitylabelsall models 4v5v, resolution 3.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4v5v is a 44 chain structure with sequence from [1] and Escherichia coli. This structure supersedes and combines the now removed PDB entries 2yhp and 2yhq. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2yhp, 2yhq Resources: FirstGlance, OCA, RCSB, PDBsum Warning: this is a large structure, and loading might take a long time or not happen at all. Publication Abstract from PubMed Respiratory syncytial virus (RSV) is a frequent cause of respiratory illness in infants, but there is currently no vaccine nor effective drug treatment against this virus. The RSV RNA genome is encapsidated and protected by a nucleocapsid protein; this RNA-nucleocapsid complex serves as a template for viral replication. Interest in the nucleocapsid protein has increased owing to its recent identification as the target site for novel anti-RSV compounds. The crystal structure of human respiratory syncytial virus nucleocapsid (HRSVN) was determined to 3.6 A resolution from two crystal forms belonging to space groups P2(1)2(1)2(1) and P1, with one and four decameric rings per asymmetric unit, respectively. In contrast to a previous structure of HRSVN, the addition of phosphoprotein was not required to obtain diffraction-quality crystals. The HRSVN structures reported here, although similar to the recently published structure, present different molecular packing which may have some biological implications. The positions of the monomers are slightly shifted in the decamer, confirming the adaptability of the ring structure. The details of the inter-ring contacts in one crystal form revealed here suggest a basis for helical packing and that the stabilization of native HRSVN is via mainly ionic interactions. Structures of respiratory syncytial virus nucleocapsid protein from two crystal forms: details of potential packing interactions in the native helical form.,El Omari K, Dhaliwal B, Ren J, Abrescia NG, Lockyer M, Powell KL, Hawkins AR, Stammers DK Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Oct 1;67(Pt, 10):1179-83. Epub 2011 Sep 24. PMID:22102022 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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