 |
PDBsum entry 6n4y
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Membrane protein
|
PDB id
|
|
|
|
6n4y
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
507 a.a.
|
|
|
|
|
|
|
|
|
|
|
480 a.a.
|
|
|
|
|
|
|
|
|
|
|
123 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Membrane protein
|
|
|
Title:
|
|
Metabotropic glutamate receptor 5 extracellular domain with nb43
|
|
Structure:
|
|
Metabotropic glutamate receptor 5. Chain: a, b, c, d. Synonym: mglur5. Engineered: yes. Nanobody 43. Chain: e, f, g, h. Engineered: yes. Other_details: nanobody 43
|
|
Source:
|
|
Homo sapiens. Human. Organism_taxid: 9606. Gene: grm5, gprc1e, mglur5. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: high five. Lama glama. Organism_taxid: 9844.
|
|
Resolution:
|
|
|
3.26Å
|
R-factor:
|
0.201
|
R-free:
|
0.251
|
|
|
Authors:
|
|
A.Koehl,H.Hu,D.Feng,B.Sun,M.Chu,W.I.Weis,J.M.Mathiesen,G.Skiniotis, B.K.Kobilka
|
|
Key ref:
|
|
A.Koehl
et al.
(2019).
Structural insights into the activation of metabotropic glutamate receptors.
Nature,
566,
79-84.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
20-Nov-18
|
Release date:
|
23-Jan-19
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P41594
(GRM5_HUMAN) -
Metabotropic glutamate receptor 5 from Homo sapiens
|
|
|
|
Seq:
Struc:
|
|
|
|
1212 a.a.
507 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Nature
566:79-84
(2019)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Structural insights into the activation of metabotropic glutamate receptors.
|
|
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.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
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.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
| |
Links
