Structure of the immature retroviral capsid at 8 angstrom resolution by cryo-electron microscopy
The result's identifiers
Result code in 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>
Alternative codes found
RIV/60461373:22330/12:43894097
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Structure of the immature retroviral capsid at 8 angstrom resolution by cryo-electron microscopy
Original language description
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
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2012
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
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Volume of the periodical
487
Issue of the periodical within the volume
7407
Country of publishing house
GB - UNITED KINGDOM
Number of pages
5
Pages from-to
385-389
UT code for WoS article
000306506500047
EID of the result in the Scopus database
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