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TitleStructural basis for CCR6 modulation by allosteric antagonists.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 7574, Year 2024
Publish dateAug 31, 2024
AuthorsDavid Jonathan Wasilko / Brian S Gerstenberger / Kathleen A Farley / Wei Li / Jennifer Alley / Mark E Schnute / Ray J Unwalla / Jorge Victorino / Kimberly K Crouse / Ru Ding / Parag V Sahasrabudhe / Fabien Vincent / Richard K Frisbie / Alpay Dermenci / Andrew Flick / Chulho Choi / Gary Chinigo / James J Mousseau / John I Trujillo / Philippe Nuhant / Prolay Mondal / Vincent Lombardo / Daniel Lamb / Barbara J Hogan / Gurdeep Singh Minhas / Elena Segala / Christine Oswald / Ian W Windsor / Seungil Han / Mathieu Rappas / Robert M Cooke / Matthew F Calabrese / Gabriel Berstein / Atli Thorarensen / Huixian Wu /
PubMed AbstractThe CC chemokine receptor 6 (CCR6) is a potential target for chronic inflammatory diseases. Previously, we reported an active CCR6 structure in complex with its cognate chemokine CCL20, revealing the ...The CC chemokine receptor 6 (CCR6) is a potential target for chronic inflammatory diseases. Previously, we reported an active CCR6 structure in complex with its cognate chemokine CCL20, revealing the molecular basis of CCR6 activation. Here, we present two inactive CCR6 structures in ternary complexes with different allosteric antagonists, CCR6/SQA1/OXM1 and CCR6/SQA1/OXM2. The oxomorpholine analogues, OXM1 and OXM2 are highly selective CCR6 antagonists which bind to an extracellular pocket and disrupt the receptor activation network. An energetically favoured U-shaped conformation in solution that resembles the bound form is observed for the active analogues. SQA1 is a squaramide derivative with close-in analogues reported as antagonists of chemokine receptors including CCR6. SQA1 binds to an intracellular pocket which overlaps with the G protein site, stabilizing a closed pocket that is a hallmark of inactive GPCRs. Minimal communication between the two allosteric pockets is observed, in contrast to the prevalent allosteric cooperativity model of GPCRs. This work highlights the versatility of GPCR antagonism by small molecules, complementing previous knowledge of CCR6 activation, and sheds light on drug discovery targeting CCR6.
External linksNat Commun / PubMed:39217154 / PubMed Central
MethodsEM (single particle)
Resolution3.02 - 3.26 Å
Structure data

46533

9d3e

EMDB-46533, PDB-9d3e:
Cryo-EM structure of CCR6 bound by SQA1 and OXM2
Method: EM (single particle) / Resolution: 3.02 Å

46534

9d3g

EMDB-46534, PDB-9d3g:
Cryo-EM structure of CCR6 bound by SQA1 and OXM1
Method: EM (single particle) / Resolution: 3.26 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

ChemComp-EBX:
4-[[3,4-bis(oxidanylidene)-2-[[(1~{R})-1-(4-propan-2-ylfuran-2-yl)propyl]amino]cyclobuten-1-yl]amino]-~{N},~{N}-dimethyl-3-oxidanyl-pyridine-2-carboxamide

PDB-1a1w:
FADD DEATH EFFECTOR DOMAIN, F25Y MUTANT, NMR MINIMIZED AVERAGE STRUCTURE

PDB-1a2a:
AGKISTROTOXIN, A PHOSPHOLIPASE A2-TYPE PRESYNAPTIC NEUROTOXIN FROM AGKISTRODON HALYS PALLAS

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / GPCR / Antagonist / CCR6 / BRIL

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