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TitleStructural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 3031, Year 2020
Publish dateJun 15, 2020
AuthorsDavid Jonathan Wasilko / Zachary Lee Johnson / Mark Ammirati / Ye Che / Matthew C Griffor / Seungil Han / Huixian Wu /
PubMed AbstractChemokines are important protein-signaling molecules that regulate various immune responses by activating chemokine receptors which belong to the G protein-coupled receptor (GPCR) superfamily. ...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.
External linksNat Commun / PubMed:32541785 / PubMed Central
MethodsEM (single particle)
Resolution3.34 Å
Structure data

21950

6wwz

EMDB-21950, PDB-6wwz:
Cryo-EM structure of the human chemokine receptor CCR6 in complex with CCL20 and a Go protein
Method: EM (single particle) / Resolution: 3.34 Å

Source
  • rattus norvegicus (Norway rat)
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / GPCR / Chemokine / Chemokine receptor / Complex

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