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Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy
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SYSNO ASEP 0383359 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Structural changes of human RNase L upon homodimerization investigated by Raman spectroscopy Author(s) Kříž, M. (CZ)
Snášel, Jan (UOCHB-X) RID
Kopecký, V. Jr. (CZ)
Páv, Ondřej (UOCHB-X) RID, ORCID
Rosenberg, Ivan (UOCHB-X) RID, ORCID
Štepánek, J. (CZ)Number of authors 6 Source Title Biochimica Et Biophysica Acta-Proteins and Proteomics. - : Elsevier - ISSN 1570-9639
Roč. 1824, č. 9 (2012), s. 1039-1044Number of pages 6 s. Language eng - English Country NL - Netherlands Keywords RNase L ; Raman spectroscopy ; DCDR spectroscopy ; phosphonate oligoadenylate ; ligand binding Subject RIV BO - Biophysics R&D Projects GA202/09/0193 GA ČR - Czech Science Foundation (CSF) KAN200520801 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) Institutional support UOCHB-X - RVO:61388963 UT WOS 000307369500005 DOI https://doi.org/10.1016/j.bbapap.2012.06.002 Annotation RNase La 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. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2013
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