Structure of the immature retroviral capsid at 8 angstrom resolution by cryo-electron microscopy

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F12%3A00381079" target="_blank" >RIV/61388963:_____/12:00381079 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22330/12:43894097

Výsledek na webu

<a href="http://dx.doi.org/10.1038/nature11169" target="_blank" >http://dx.doi.org/10.1038/nature11169</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/nature11169" target="_blank" >10.1038/nature11169</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structure of the immature retroviral capsid at 8 angstrom resolution by cryo-electron microscopy

Popis výsledku v původním jazyce

The assembly of retroviruses such as HIV-1 is driven by oligomerization of their major structural protein, Gag. Gag is a multi-domain polyprotein including three conserved folded domains MA (matrix), CA (capsid) and NC (nucleocapsid). Assembly of an infectious virion proceeds in two stages. In the first stage, Gag oligomerization into a hexameric protein lattice leads to formation of an incomplete, roughly spherical protein shell that buds through the plasma membrane of the infected cell to release an enveloped immature virus particle. In the second stage, cleavage of Gag by the viral protease leads to rearrangement of the particle interior, converting the non-infectious immature virus particle into a mature infectious virion. The immature Gag shell acts as the pivotal intermediate in assembly and is a potential target for anti-retroviral drugs both to inhibit virus assembly and to disrupt virus maturation. Detailed structural information on the immature Gag shell has not been availabl

Název v anglickém jazyce

Structure of the immature retroviral capsid at 8 angstrom resolution by cryo-electron microscopy

Popis výsledku anglicky

The assembly of retroviruses such as HIV-1 is driven by oligomerization of their major structural protein, Gag. Gag is a multi-domain polyprotein including three conserved folded domains MA (matrix), CA (capsid) and NC (nucleocapsid). Assembly of an infectious virion proceeds in two stages. In the first stage, Gag oligomerization into a hexameric protein lattice leads to formation of an incomplete, roughly spherical protein shell that buds through the plasma membrane of the infected cell to release an enveloped immature virus particle. In the second stage, cleavage of Gag by the viral protease leads to rearrangement of the particle interior, converting the non-infectious immature virus particle into a mature infectious virion. The immature Gag shell acts as the pivotal intermediate in assembly and is a potential target for anti-retroviral drugs both to inhibit virus assembly and to disrupt virus maturation. Detailed structural information on the immature Gag shell has not been availabl

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Nature

ISSN

0028-0836

e-ISSN

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Svazek periodika

487

Číslo periodika v rámci svazku

7407

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

5

Strana od-do

385-389

Kód UT WoS článku

000306506500047

EID výsledku v databázi Scopus

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