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PDBsum entry 2oj4
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Signaling protein inhibitor
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PDB id
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2oj4
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References listed in PDB file
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Key reference
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Title
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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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Authors
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L.Rezabkova,
E.Boura,
P.Herman,
J.Vecer,
L.Bourova,
M.Sulc,
P.Svoboda,
V.Obsilova,
T.Obsil.
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Ref.
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J Struct Biol, 2010,
170,
451-461.
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PubMed id
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Abstract
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Regulator of G protein signaling (RGS) proteins function as GTPase-activating
proteins (GAPs) for the alpha-subunit of heterotrimeric G proteins. Several RGS
proteins have been found to interact with 14-3-3 proteins. The 14-3-3 protein
binding inhibits the GAP function of RGS proteins presumably by blocking their
interaction with G(alpha) subunit. Since RGS proteins interact with G(alpha)
subunits through their RGS domains, it is reasonable to assume that the 14-3-3
protein can either sterically occlude the G(alpha) interaction surface of RGS
domain and/or change its structure. In this work, we investigated whether the
14-3-3 protein binding affects the structure of RGS3 using the time-resolved
tryptophan fluorescence spectroscopy. Two single-tryptophan mutants of RGS3 were
used to study conformational changes of RGS3 molecule. Our measurements 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.
Experiments with the isolated RGS domain of RGS3 suggest that this domain alone
can, to some extent, interact with the 14-3-3 protein in a
phosphorylation-independent manner. In addition, a crystal structure of the RGS
domain of RGS3 was solved at 2.3A resolution. The data obtained from the
resolution of the 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.
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