14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3)

0343365 - FGÚ 2011 RIV US eng J - Journal Article
Řežábková, L. - Bouřa, E. - Herman, P. - Večeř, J. - Bouřová, Lenka - Šulc, Miroslav - Svoboda, Petr - Obšilová, Veronika - Obšil, T.
14-3-3 protein interacts with and affects the structure of RGS domain of regulator of G protein signaling 3 (RGS3).
Journal of Structural Biology. Roč. 170, č. 3 (2010), s. 451-461. ISSN 1047-8477. E-ISSN 1095-8657
R&D Projects: GA MŠMT(CZ) LC554; GA AV ČR(CZ) IAA501110801
Institutional research plan: CEZ:AV0Z50110509; CEZ:AV0Z50200510
Keywords : 14-3-3 protein * time-resolved fluorescence * RGS3
Subject RIV: BO - Biophysics
Impact factor: 3.497, year: 2010

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
Permanent Link: http://hdl.handle.net/11104/0185864