Inflammation is a normal response to any injury or infection. However, sustained inflammation can cause numerous diseases. A hallmark of inflammation is leukocyte recruitment to the affected tissue, regulated by small secretory proteins called chemokines. They bind and activate chemokine receptors expressed on the leukocyte surface (1). As a strategy to suppress detection and prolong their feeding time, ticks produce chemokine-binding proteins called 'Evasins', which bind to host chemokines and block chemokine receptors' activation preventing leukocyte migration. Several studies have shown that Evasins are natural, selective chemokine-inhibitory proteins with excellent potential as therapeutics for inflammatory diseases (2,3). Using bioinformatics, we identified variants of previously characterised Evasins with ten cysteine residues forming five-disulfide bonds. We expressed and purified EVA-ACA1001 using the E. coli expression system and analysis of the purified protein supported the predicted five intramolecular disulfide bonds. Binding data, obtained using a surface plasmon resonance (SPR), showed that EVA-ACA1001 binds to multiple CC chemokines with dissociation equilibrium constants (KD) in the range (0.01-100) nM. Furthermore, cAMP inhibition assay demonstrated the chemokine inhibitory function with IC50 value (1 nM to 100 nM). Truncation of N and C terminus confirmed that the core region confers the chemokine binding and selectivity of EVA-ACA1001, a distinct feature of C10 Evasins. Our crystal structures of a C10 Evasin in complex with the chemokines CCL7 and CCL17 showed extensive hydrogen bonds between Evasin and the CC motif of chemokine, a common feature of Class A Evasins. In contrast to traditional Class A Evasins, a big hydrophobic pocket formed in the core region of C10 Evasin can accommodate at least two amino residues from the N- loop of chemokines, making it a broad binder. Thus, this study describes structure and function of C10 Evasins and pave a pathway for the engineering of a potent anti-inflammatory molecules.