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14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3)
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SYSNO ASEP 0343365 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title 14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3) Author(s) Řežábková, L. (CZ)
Bouřa, E. (CZ)
Herman, P. (CZ)
Večeř, J. (CZ)
Bouřová, Lenka (FGU-C)
Šulc, Miroslav (MBU-M) RID, ORCID
Svoboda, Petr (FGU-C) RID, ORCID
Obšilová, Veronika (FGU-C) RID, ORCID, SAI
Obšil, T. (CZ)Source Title Journal of Structural Biology. - : Elsevier - ISSN 1047-8477
Roč. 170, č. 3 (2010), s. 451-461Number of pages 11 s. Language eng - English Country US - United States Keywords 14-3-3 protein ; time-resolved fluorescence ; RGS3 Subject RIV BO - Biophysics R&D Projects LC554 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) IAA501110801 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) CEZ AV0Z50110509 - FGU-C (2005-2011) AV0Z50200510 - MBU-M (2005-2011) UT WOS 000277946200003 DOI 10.1016/j.jsb.2010.03.009 Annotation We have investigated whether the 14-3-3 protein binding affects the structure of RGS3 using the time-resolved tryptophan fluorescence spectroscopy and X-ray protein crystallography. Our results revealed that the 14-3-3 protein binding induces structural changes in both the N-terminal part and the C-terminal RGS domain of phosphorylated RGS3 molecule. The data obtained from the resolution of the crystal structure of the RGS domain suggest that the 14-3-3 protein-induced conformational change affects the region within the G(alpha)-interacting portion of the RGS domain. This can explain the inhibitory effect of the 14-3-3 protein on GAP activity of RGS3 Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2011
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