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

Result code in 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>
Alternative codes found
RIV/61388963:_____/12:00383359
Result on the web
<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>

Result language
angličtina
Original language name
Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy
Original language description
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
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
BO - Biophysics
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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