Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F12%3A10125473" target="_blank" >RIV/00216208:11320/12:10125473 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388963:_____/12:00383359

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.bbapap.2012.06.002" target="_blank" >http://dx.doi.org/10.1016/j.bbapap.2012.06.002</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbapap.2012.06.002" target="_blank" >10.1016/j.bbapap.2012.06.002</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy

Popis výsledku v původním jazyce

RNase L, a key enzyme in the host defense system, is activated by the binding of 2'-5'-linked oligoadenylates (2-5A) to the N-terminal ankyrin repeat domain, which causes the inactive monomer to form a catalytically active homodimer. We focused on the structural changes of human RNase L as a result of interactions with four different activators: natural 2-5 pA(4) and three tetramers with 3'-end AMP units replaced with ribo-, arabino- and xylo-configured phosphonate analogs of AMP (pA(3)X). The extent ofthe RNase L dimerization and its cleavage activity upon binding of all these activators were similar. A drop-coating deposition Raman (DCDR) spectroscopy possessed uniform spectral changes upon binding of all of the tetramers, which verified the same binding mechanism. The estimated secondary structural composition of monomeric RNase L is 44% alpha-helix, 28% beta-sheet, 17% beta-turns and 11% of unordered structures, whereas dimerization causes a slight decrease in alpha-helix and incr

Název v anglickém jazyce

Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy

Popis výsledku anglicky

RNase L, a key enzyme in the host defense system, is activated by the binding of 2'-5'-linked oligoadenylates (2-5A) to the N-terminal ankyrin repeat domain, which causes the inactive monomer to form a catalytically active homodimer. We focused on the structural changes of human RNase L as a result of interactions with four different activators: natural 2-5 pA(4) and three tetramers with 3'-end AMP units replaced with ribo-, arabino- and xylo-configured phosphonate analogs of AMP (pA(3)X). The extent ofthe RNase L dimerization and its cleavage activity upon binding of all these activators were similar. A drop-coating deposition Raman (DCDR) spectroscopy possessed uniform spectral changes upon binding of all of the tetramers, which verified the same binding mechanism. The estimated secondary structural composition of monomeric RNase L is 44% alpha-helix, 28% beta-sheet, 17% beta-turns and 11% of unordered structures, whereas dimerization causes a slight decrease in alpha-helix and incr

Druh

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

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

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

Název periodika

Biochimica et Biophysica Acta - Proteins and Proteomics

ISSN

1570-9639

e-ISSN

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Svazek periodika

1824

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

6

Strana od-do

1039-1044

Kód UT WoS článku

000307369500005

EID výsledku v databázi Scopus

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