Selected article for: "overall structure and similar overall structure"
Author: Zivcec, Marko; Scholte, Florine E. M.; Spiropoulou, Christina F.; Spengler, Jessica R.; Bergeron, Éric
Title: Molecular Insights into Crimean-Congo Hemorrhagic Fever Virus
  • Document date: 2016_4_21
    • ID: 0a20s62q_20
    Snippet: Important insights into the roles of NP were obtained from the crystal structures of CCHFV NP using CCHFV isolates from Iraq [65] and China [66, 67] . The protein structure is more closely related to the NP of arenaviruses [68, 69] than to that of NP of other bunyaviruses [70] [71] [72] . The NP possesses two major domains: a globular head and a flexible arm. The arm domain protrudes from the globular head domain of CCHFV NP. The globular head do.....
    Document: Important insights into the roles of NP were obtained from the crystal structures of CCHFV NP using CCHFV isolates from Iraq [65] and China [66, 67] . The protein structure is more closely related to the NP of arenaviruses [68, 69] than to that of NP of other bunyaviruses [70] [71] [72] . The NP possesses two major domains: a globular head and a flexible arm. The arm domain protrudes from the globular head domain of CCHFV NP. The globular head domain of CCHFV NP comprises 23 α-helices with an overall structure that is similar to the NP of Lassa virus (LASV), an arenavirus. Crystallization of NP as an oligomer in the presence of RNA demonstrated that NP subunits organize in a head-to-tail orientation, with the arm of one subunit interacting with the head domain of the neighboring subunit, that are further assembled into double antiparallel superhelical polymers of NP; this may represent the organization of NP in the RNPs [73] .

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