1H, 13C, 15N assignment and secondary structure identification of the 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%3A00004694" target="_blank" >RIV/60461373:22640/01:00004694 - 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

1H, 13C, 15N assignment and secondary structure identification of the protease from Mason-Pfizer Monkey Virus

Popis výsledku v původním jazyce

NMason-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

1H, 13C, 15N assignment and secondary structure identification of the protease from Mason-Pfizer Monkey Virus

Popis výsledku anglicky

NMason-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

D - Stať ve sborníku

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 statě ve sborníku

Central European NMR Discussion Groups

ISBN

80-210-2566-2

ISSN

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e-ISSN

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Počet stran výsledku

1

Strana od-do

30

Název nakladatele

Masarykova univerzita Brno

Místo vydání

Neuveden

Místo konání akce

Valtice, ČR

Datum konání akce

23. 4. 2001

Typ akce podle státní příslušnosti

EUR - Evropská akce

Kód UT WoS článku

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