Backbone dynamics of the CC‐chemokine eotaxin‐2 and comparison among the eotaxin group chemokines

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Abstract
The eotaxin group chemokines (eotaxin, eotaxin‐2, and eotaxin‐3) share only 35–41% sequence identity but are all agonists for the receptor CCR3. Here we present a detailed comparison between the backbone dynamics of these three chemokines. The dynamics of eotaxin‐2 were determined from 15N NMR relaxation data and compared to those obtained previously for eotaxin and eotaxin‐3. For all three chemokines, the majority of residues in the first two β‐strands and the α‐helix show highly restricted motions on the subnanosecond time scale but there is dramatically higher flexibility in the N‐ and C‐terminal regions and also substantial mobility for residues in the N‐loop region and the third β‐strand. The latter two regions form a groove on the chemokine surface that is the likely binding site for the N‐terminal region of the receptor. Taken together, the available data suggest a model in which conformational rearrangements of both the chemokine and the receptor are likely to occur during binding and receptor activation. Proteins 2003;50:184–191.