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| rdf:type
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| rdfs:seeAlso
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| 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 of the 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 increase in beta-sheet (ca. 2%) content. The dimerization affects at least three Tyr, five Phe and two Trp residues. The alpha-beta structural switch may fix domain positions in the hinge region (residues ca. 336-363) during homodimer formation. (C) 2012 Elsevier B.V. All rights reserved.
- 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 of the 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 increase in beta-sheet (ca. 2%) content. The dimerization affects at least three Tyr, five Phe and two Trp residues. The alpha-beta structural switch may fix domain positions in the hinge region (residues ca. 336-363) during homodimer formation. (C) 2012 Elsevier B.V. All rights reserved. (en)
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| Title
| - Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy
- Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy (en)
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| skos:prefLabel
| - Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy
- Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy (en)
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| skos:notation
| - RIV/00216208:11320/12:10125473!RIV13-AV0-11320___
|
| http://linked.open...avai/predkladatel
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
| - I, P(GA202/09/0193), P(KAN200520801), P(KJB101120805)
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| http://linked.open...iv/cisloPeriodika
| |
| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
| |
| http://linked.open.../riv/druhVysledku
| |
| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/00216208:11320/12:10125473
|
| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - ligand binding; phosphonate oligoadenylate; DCDR spectroscopy; Raman spectroscopy; RNase L (en)
|
| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
| |
| http://linked.open...ontrolniKodProRIV
| |
| http://linked.open...i/riv/nazevZdroje
| - Biochimica et Biophysica Acta - Proteins and Proteomics
|
| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
| |
| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...vavai/riv/projekt
| |
| http://linked.open...UplatneniVysledku
| |
| http://linked.open...v/svazekPeriodika
| |
| http://linked.open...iv/tvurceVysledku
| - Rosenberg, Ivan
- Štěpánek, Josef
- Kopecký, Vladimír
- Kříž, Martin
- Pav, Ondrej
- Snasel, Jan
|
| http://linked.open...ain/vavai/riv/wos
| |
| issn
| |
| number of pages
| |
| http://bibframe.org/vocab/doi
| - 10.1016/j.bbapap.2012.06.002
|
| http://localhost/t...ganizacniJednotka
| |
| is http://linked.open...avai/riv/vysledek
of | |
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