8fk9 | pdb_00008fk9

Crystal Structure of the Tick Evasin EVA-ACA1001 Complexed to Human Chemokine CCL16

spinqualitylabelsall models 8fk9, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8fk9 is a 4 chain structure with sequence from Amblyomma cajennense and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EV991_AMBCJ Salivary chemokine-binding protein which has chemokine-neutralizing activity and binds to host chemokines CCL2, CCL3, CCL3L1, CCL4, CCL4L1, CCL5, CCL6, CCL7, CCL8, CCL9, CCL11, CCL12, CCL13, CCL14, CCL16, CCL17, CCL18, CCL19, CCL22, CCL23, CCL24 and CCL27. Publication Abstract from PubMed Ticks produce chemokine-binding proteins, known as evasins, in their saliva to subvert the host's immune response. Evasins bind to chemokines and thereby inhibit the activation of their cognate chemokine receptors, thus suppressing leukocyte recruitment and inflammation. We recently described subclass A3 evasins, which, like other class A evasins, exclusively target CC chemokines but appear to use a different binding site architecture to control target selectivity among CC chemokines. We now describe the structural basis of chemokine recognition by the class A3 evasin EVA-ACA1001. EVA-ACA1001 binds to almost all human CC chemokines and inhibits receptor activation. Truncation mutants of EVA-ACA1001 showed that, unlike class A1 evasins, both the N- and C-termini of EVA-ACA1001 play minimal roles in chemokine binding. To understand the structural basis of its broad chemokine recognition, we determined the crystal structure of EVA-ACA1001 in complex with the human chemokine CCL16. EVA-ACA1001 forms backbone-backbone interactions with the CC motif of CCL16, a conserved feature of all class A evasin-chemokine complexes. A hydrophobic pocket in EVA-ACA1001, formed by several aromatic side chains and the unique disulfide bond of class A3 evasins, accommodates the residue immediately following the CC motif (the "CC + 1 residue") of CCL16. This interaction is shared with EVA-AAM1001, the only other class A3 evasins characterized to date, suggesting it may represent a common mechanism that accounts for the broad recognition of CC chemokines by class A3 evasins. Structural basis of chemokine recognition by the class A3 tick evasin EVA-ACA1001.,Devkota SR, Aryal P, Wilce MCJ, Payne RJ, Stone MJ, Bhusal RP Protein Sci. 2024 Jun;33(6):e4999. doi: 10.1002/pro.4999. PMID:38723106 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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