Fig. 1: Cryo-EM structure of the CCR6/CCL20–Go–scFv16 complex and comparison with other chemokine–GPCR complexes.
From: Structural basis for chemokine receptor CCR6 activation by the endogenous protein ligand CCL20
a Orthogonal and extracellular views of the cryo-EM map of the CCR6/CCL20–Go heterotrimer complex colored by subunit. CCR6, light magenta; CCL20, yellow; Gαo Ras-like domain, green; Gβ, cyan; Gγ, orange; scFv16, gray. b Model of the CCR6/CCL20–Go complex in the same views and color scheme as shown in (a). c Overlay with other known inactive chemokine–chemokine receptor complex structures reveals massive diversity in chemokine binding mode (CCR5/[5P7]CCL5, CXCR4/vMIP-II, US28/CX3CL). d Comparison of the depth into which each chemokine N terminus reaches in the orthosteric pocket of its cognate receptor. CCL20 binds in a shallow pocket at the extracellular surface with minimal contact to the 7TM core. Heavy dotted lines highlight the membrane boundaries, and light dotted line is the deepest chemokine binding position revealed by US28/CX3CL1 complex structure.
