Backbone resonance assignment of protease from Mason-Pfizer monkey virus

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22640%2F01%3A00004693" target="_blank" >RIV/60461373:22640/01:00004693 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Backbone resonance assignment of protease from Mason-Pfizer monkey virus

Popis výsledku v původním jazyce

Mason-Pfizer monkey virus encodes an aspartic protease (M-PMV PR), which is essential for the maturation of the virion particles by processing viral protein precursors yielding fully functional structural proteins and enzymes. The overall fold of all known retroviral proteases is quite conservative despite rather large varieties of their amino acid sequences. However, Mason-Pfizer Monkey Virus protease exists in three active forms, which is a feature making this enzyme unique within the this family. Invivo Mason-Pfizer Monkey Virus protease occurs as a 17 kDa (per monomer) molecule. In vitro it undergoes a rapid self-processing at the C-terminus yielding 13 kDa and finally 12 kDa forms [1]. We will present backbone resonance assignment and secondary structure identification of shortest 12 kDa form of protease from Mason-Pfizer Monkey Virus [2].

Název v anglickém jazyce

Backbone resonance assignment of protease from Mason-Pfizer monkey virus

Popis výsledku anglicky

Mason-Pfizer monkey virus encodes an aspartic protease (M-PMV PR), which is essential for the maturation of the virion particles by processing viral protein precursors yielding fully functional structural proteins and enzymes. The overall fold of all known retroviral proteases is quite conservative despite rather large varieties of their amino acid sequences. However, Mason-Pfizer Monkey Virus protease exists in three active forms, which is a feature making this enzyme unique within the this family. Invivo Mason-Pfizer Monkey Virus protease occurs as a 17 kDa (per monomer) molecule. In vitro it undergoes a rapid self-processing at the C-terminus yielding 13 kDa and finally 12 kDa forms [1]. We will present backbone resonance assignment and secondary structure identification of shortest 12 kDa form of protease from Mason-Pfizer Monkey Virus [2].

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GA203%2F00%2F1241" target="_blank" >GA203/00/1241: Biologické a strukturní studie proteasy Mason-Pfizerova opičího viru</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2001

Kód důvěrnosti údajů

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

Název periodika

Journal of Biomolecular NMR

ISSN

0925-2738

e-ISSN

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Svazek periodika

20

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

2

Strana od-do

291-292

Kód UT WoS článku

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EID výsledku v databázi Scopus

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