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PDBsum entry 4ekd
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Signaling protein/inhibitor
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PDB id
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4ekd
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References listed in PDB file
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Key reference
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Title
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Structural and functional analysis of the regulator of g protein signaling 2-Gαq complex.
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Authors
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M.R.Nance,
B.Kreutz,
V.M.Tesmer,
R.Sterne-Marr,
T.Kozasa,
J.J.Tesmer.
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Ref.
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Structure, 2013,
21,
438-448.
[DOI no: ]
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PubMed id
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Abstract
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The heterotrimeric G protein Gαq is a key regulator of blood pressure, and
excess Gαq signaling leads to hypertension. A specific inhibitor of Gαq is the
GTPase activating protein (GAP) known as regulator of G protein signaling 2
(RGS2). The molecular basis for how Gαq/11 subunits serve as substrates for RGS
proteins and how RGS2 mandates its selectivity for Gαq is poorly understood.
In crystal structures of the RGS2-Gαq complex, RGS2 docks to Gαq in a
different orientation from that observed in RGS-Gαi/o complexes. Despite its
unique pose, RGS2 maintains canonical interactions with the switch regions of
Gαq in part because its α6 helix adopts a distinct conformation. We show that
RGS2 forms extensive interactions with the α-helical domain of Gαq that
contribute to binding affinity and GAP potency. RGS subfamilies that do not
serve as GAPs for Gαq are unlikely to form analogous stabilizing interactions.
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