High-resolution structure of a retroviral protease folded as a monomer

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F11%3A00369861" target="_blank" >RIV/61388963:_____/11:00369861 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1107/S0907444911035943" target="_blank" >http://dx.doi.org/10.1107/S0907444911035943</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S0907444911035943" target="_blank" >10.1107/S0907444911035943</a>

Jazyk výsledku

angličtina

Název v původním jazyce

High-resolution structure of a retroviral protease folded as a monomer

Popis výsledku v původním jazyce

Biophysical and NMR studies of M-PMV protease have indicated that in the absence of substrates or inhibitors M-PMV PR should fold into a stable monomer, but the crystal structure of this protein could not be solved by molecular replacement despite countless attempts. The solution was obtained in mr-rosetta using a model constructed by players of the game Foldit. The structure shows a monomeric protein, with the N- and C-termini completely disordered. The flap loop has an unusual curled shape and a different orientation from both the open and closed states known from dimeric retropepsins. This structure provides important information for the design of dimerization inhibitors of retroviral proteases.

Název v anglickém jazyce

High-resolution structure of a retroviral protease folded as a monomer

Popis výsledku anglicky

Biophysical and NMR studies of M-PMV protease have indicated that in the absence of substrates or inhibitors M-PMV PR should fold into a stable monomer, but the crystal structure of this protein could not be solved by molecular replacement despite countless attempts. The solution was obtained in mr-rosetta using a model constructed by players of the game Foldit. The structure shows a monomeric protein, with the N- and C-termini completely disordered. The flap loop has an unusual curled shape and a different orientation from both the open and closed states known from dimeric retropepsins. This structure provides important information for the design of dimerization inhibitors of retroviral proteases.

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/1M0508" target="_blank" >1M0508: Nová antivirotika a antineoplastika</a><br>

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

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

Název periodika

Acta Crystallographica Section D-Biological Crystallography

ISSN

0907-4449

e-ISSN

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Svazek periodika

D67

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

DK - Dánské království

Počet stran výsledku

8

Strana od-do

907-914

Kód UT WoS článku

000296787400001

EID výsledku v databázi Scopus

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