Conformational plasticity and dynamic interactions of the N-terminal domain of the chemokine receptor CXCR1
Fig 6
Binding modes of IL8 characterizing its interactions with the N-terminal region of CXCR1.
(A) The most populated binding modes of IL8 characterized by the contacts formed by each of its structural element with the N-terminal region of CXCR1. The structural elements are denoted as I: N-domain, II: β1-strand, III: β2-strand, IV: β3-strand, and V: α-helix. The binding modes are numbered 1 to 5, in decreasing order of population. The green and red boxes represent interacting and non-interacting regions, respectively. (B) IL8 residues involved in binding to CXCR1 mapped on the cartoon representation of IL8. The cyan spheres represent interacting residues identified from our simulations. The orange and violet spheres represent interacting residues determined from previous NMR [37,42] and mutagenesis [43–47] studies, respectively. See Methods and text for more details.