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Structure of the immature HIV-1 capsid in intact virus particles at 8.8 angstrom resolution

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F15%3A00443186" target="_blank" >RIV/61388963:_____/15:00443186 - isvavai.cz</a>

  • Alternative codes found

    RIV/60461373:22330/15:43899648

  • Result on the web

    <a href="http://dx.doi.org/10.1038/nature13838" target="_blank" >http://dx.doi.org/10.1038/nature13838</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/nature13838" target="_blank" >10.1038/nature13838</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Structure of the immature HIV-1 capsid in intact virus particles at 8.8 angstrom resolution

  • Original language description

    Human immunodeficiency virus type 1 (HIV-1) assembly proceeds in two stages. First, the 55 kilodalton viral Gag polyprotein assembles into a hexameric protein lattice at the plasma membrane of the infected cell, inducing budding and release of an immature particle. Second, Gag is cleaved by the viral protease, leading to internal rearrangement of the virus into the mature, infectious form(1). Immature and mature HIV-1 particles are heterogeneous in size and morphology, preventing high-resolution analysis of their protein arrangement in situ by conventional structural biology methods. Here we apply cryo-electron tomography and sub -tomogram averaging methods to resolve the structure of the capsid lattice within intact immature HIV-1 particles at subnanometre resolution, allowing unambiguous positioning of all alpha-helices. The resulting model reveals tertiary and quaternary structural interactions that mediate HIV-1 assembly. Strikingly, these interactions differ from those predicted b

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GA14-15326S" target="_blank" >GA14-15326S: Study of structure and interactions critical for formation of immature retroviral particles for testing and rational design of HIV assembly inhibitors</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Nature

  • ISSN

    0028-0836

  • e-ISSN

  • Volume of the periodical

    517

  • Issue of the periodical within the volume

    7535

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    4

  • Pages from-to

    505-508

  • UT code for WoS article

    000348196500039

  • EID of the result in the Scopus database

    2-s2.0-84924189026