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PDBsum entry 6wwz
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Membrane protein
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PDB id
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6wwz
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Contents |
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338 a.a.
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66 a.a.
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56 a.a.
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210 a.a.
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231 a.a.
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310 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 basis for chemokine receptor ccr6 activation by the endogenous protein ligand ccl20.
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Authors
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D.J.Wasilko,
Z.L.Johnson,
M.Ammirati,
Y.Che,
M.C.Griffor,
S.Han,
H.Wu.
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Ref.
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Nat Commun, 2020,
11,
3031.
[DOI no: ]
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PubMed id
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Abstract
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Chemokines are important protein-signaling molecules that regulate various
immune responses by activating chemokine receptors which belong to the G
protein-coupled receptor (GPCR) superfamily. Despite the substantial progression
of our structural understanding of GPCR activation by small molecule and peptide
agonists, the molecular mechanism of GPCR activation by protein agonists remains
unclear. Here, we present a 3.3-Å cryo-electron microscopy structure of the
human chemokine receptor CCR6 bound to its endogenous ligand CCL20 and an
engineered Go. CCL20 binds in a shallow extracellular pocket, making limited
contact with the core 7-transmembrane (TM) bundle. The structure suggests that
this mode of binding induces allosterically a rearrangement of a noncanonical
toggle switch and the opening of the intracellular crevice for G protein
coupling. Our results demonstrate that GPCR activation by a protein agonist does
not always require substantial interactions between ligand and the 7TM core
region.
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