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PDBsum entry 6n4y
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Membrane protein
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PDB id
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6n4y
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Contents |
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507 a.a.
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480 a.a.
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123 a.a.
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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 insights into the activation of metabotropic glutamate receptors.
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Authors
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A.Koehl,
H.Hu,
D.Feng,
B.Sun,
Y.Zhang,
M.J.Robertson,
M.Chu,
T.S.Kobilka,
T.Laermans,
J.Steyaert,
J.Tarrasch,
S.Dutta,
R.Fonseca,
W.I.Weis,
J.M.Mathiesen,
G.Skiniotis,
B.K.Kobilka.
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Ref.
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Nature, 2019,
566,
79-84.
[DOI no: ]
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PubMed id
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Abstract
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Metabotropic glutamate receptors are family C G-protein-coupled receptors. They
form obligate dimers and possess extracellular ligand-binding Venus flytrap
domains, which are linked by cysteine-rich domains to their 7-transmembrane
domains. Spectroscopic studies show that signalling is a dynamic process, in
which large-scale conformational changes underlie the transmission of signals
from the extracellular Venus flytraps to the G protein-coupling domains-the
7-transmembrane domains-in the membrane. Here, using a combination of X-ray
crystallography, cryo-electron microscopy and signalling studies, we present a
structural framework for the activation mechanism of metabotropic glutamate
receptor subtype 5. Our results show that agonist binding at the Venus flytraps
leads to a compaction of the intersubunit dimer interface, thereby bringing the
cysteine-rich domains into close proximity. Interactions between the
cysteine-rich domains and the second extracellular loops of the receptor enable
the rigid-body repositioning of the 7-transmembrane domains, which come into
contact with each other to initiate signalling.
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