Author: Deshpande, Ashlesha; Wang, Sifang; Walsh, Martin A.; Dokland, Terje
Title: Structure of the equine arteritis virus nucleocapsid protein reveals a dimer–dimer arrangement Cord-id: 3aya6xil Document date: 2007_4_24
ID: 3aya6xil
Snippet: Equine arteritis virus (EAV) is an enveloped positiveâ€sense RNA virus belonging to the Arteriviridae family, which also includes the porcine pathogen PRRSV and is genetically and structurally related to the coronaviruses. EAV is an important equine pathogen that has caused significant economic losses to the horseâ€breeding industry and has been difficult to control. The EAV virion consists of a genomeâ€containing nucleocapsid core made of nucleocapsid (N) protein surrounded by a lipid envelo
Document: Equine arteritis virus (EAV) is an enveloped positiveâ€sense RNA virus belonging to the Arteriviridae family, which also includes the porcine pathogen PRRSV and is genetically and structurally related to the coronaviruses. EAV is an important equine pathogen that has caused significant economic losses to the horseâ€breeding industry and has been difficult to control. The EAV virion consists of a genomeâ€containing nucleocapsid core made of nucleocapsid (N) protein surrounded by a lipid envelope containing several membrane proteins. Here, the crystal structure of the capsidâ€forming domain of the EAV N protein is presented at 2.0 Ã… resolution. The dimeric Nâ€Âprotein structure is similar to the previously determined structure of the N protein from PRRSV, with most differences localized to the terminal helices and flexible loops. The N protein is organized as dimers of dimers in the crystal, which may reflect the arrangement of the protein in the viral nucleocapsid.
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