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PDBsum entry 6fuf
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Signaling protein
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PDB id
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6fuf
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References listed in PDB file
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Key reference
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Title
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Crystal structure of rhodopsin in complex with a mini-Go sheds light on the principles of g protein selectivity.
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Authors
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C.J.Tsai,
F.Pamula,
R.Nehmé,
J.Mühle,
T.Weinert,
T.Flock,
P.Nogly,
P.C.Edwards,
B.Carpenter,
T.Gruhl,
P.Ma,
X.Deupi,
J.Standfuss,
C.G.Tate,
G.F.X.Schertler.
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Ref.
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Sci Adv, 2018,
4,
eaat7052.
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PubMed id
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Abstract
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Selective coupling of G protein (heterotrimeric guanine nucleotide-binding
protein)-coupled receptors (GPCRs) to specific Gα-protein subtypes is critical
to transform extracellular signals, carried by natural ligands and clinical
drugs, into cellular responses. At the center of this transduction event lies
the formation of a signaling complex between the receptor and G protein. We
report the crystal structure of light-sensitive GPCR rhodopsin bound to an
engineered mini-Go protein. The conformation of the receptor is
identical to all previous structures of active rhodopsin, including the complex
with arrestin. Thus, rhodopsin seems to adopt predominantly one
thermodynamically stable active conformation, effectively acting like a
"structural switch," allowing for maximum efficiency in the visual
system. Furthermore, our analysis of the well-defined GPCR-G protein interface
suggests that the precise position of the carboxyl-terminal
"hook-like" element of the G protein (its four last residues) relative
to the TM7/helix 8 (H8) joint of the receptor is a significant determinant in
selective G protein activation.
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