Stabilization of the beta-hairpin in Mason-Pfizer Stabilization of the beta-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F14%3A43897364" target="_blank" >RIV/60461373:22330/14:43897364 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1186/s12977-014-0094-8" target="_blank" >http://dx.doi.org/10.1186/s12977-014-0094-8</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1186/s12977-014-0094-8" target="_blank" >10.1186/s12977-014-0094-8</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Stabilization of the beta-hairpin in Mason-Pfizer Stabilization of the beta-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity

Popis výsledku v původním jazyce

Formation of a mature core is a crucial event for infectivity of retroviruses such as Mason-Pfizer monkey virus (M-PMV). The process is triggered by proteolytic cleavage of the polyprotein precursor Gag, which releases matrix, capsid (CA), and nucleocapsid proteins. Once released, CA assembles to form a mature core - a hexameric lattice protein shell that protects retroviral genomic RNA. Subtle conformational changes within CA induce the transition from the immature lattice to the mature lattice. Upon release from the precursor, the initially unstructured N-terminus of CA is refolded to form a beta-hairpin stabilized by a salt bridge between the N-terminal proline and conserved aspartate. Although the crucial role of the beta-hairpin in the mature coreassembly has been confirmed, its precise structural function remains poorly understood.

Název v anglickém jazyce

Stabilization of the beta-hairpin in Mason-Pfizer Stabilization of the beta-hairpin in Mason-Pfizer monkey virus capsid protein- a critical step for infectivity

Popis výsledku anglicky

Formation of a mature core is a crucial event for infectivity of retroviruses such as Mason-Pfizer monkey virus (M-PMV). The process is triggered by proteolytic cleavage of the polyprotein precursor Gag, which releases matrix, capsid (CA), and nucleocapsid proteins. Once released, CA assembles to form a mature core - a hexameric lattice protein shell that protects retroviral genomic RNA. Subtle conformational changes within CA induce the transition from the immature lattice to the mature lattice. Upon release from the precursor, the initially unstructured N-terminus of CA is refolded to form a beta-hairpin stabilized by a salt bridge between the N-terminal proline and conserved aspartate. Although the crucial role of the beta-hairpin in the mature coreassembly has been confirmed, its precise structural function remains poorly understood.

Druh

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

CEP obor

EI - Biotechnologie a bionika

OECD FORD obor

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Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

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

Název periodika

Retrovirology

ISSN

1742-4690

e-ISSN

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Svazek periodika

11

Číslo periodika v rámci svazku

94

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

14

Strana od-do

1-15

Kód UT WoS článku

000344571100001

EID výsledku v databázi Scopus

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