6qjb

Truncated Evasin-3 (tEv3 17-56)

spinqualitylabelsall models 6qjb Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qjb is a 1 chain structure with sequence from Rhipicephalus sanguineus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EVA3_RHISA Publication Abstract from PubMed Chemokines are a group of chemotaxis proteins that regulate cell trafficking and play important roles in immune responses and inflammation. Ticks are blood-sucking parasites that secrete numerous immune-modulatory agents in their saliva to evade host immune responses. Evasin-3 is a small salivary protein which belongs to a class of chemokine-binding proteins isolated from the brown dog tick, Rhipicephalus sanguineus. Evasin-3 has been shown to have a high affinity for chemokines CXCL1 and CXCL8 and diminish inflammation in mice. In the present study, solution NMR spectroscopy was used to investigate the structure of Evasin-3 and its CXCL8/Evasin-3 complex. Evasin-3 is found to disrupt the glycosaminoglycan (GAG) binding site of CXCL8 and inhibit the interaction of CXCL8 with CXCR2. Structural data were used to design two novel CXCL8 binding peptides. Linear tEv3 17-56 and cyclic tcEv3 16-56 dPG Evasin-3 variants were chemically synthesized by solid phase peptide synthesis. Affinity of these newly synthesized variants to CXCL8 were measured by surface plasmon resonance (SPR) biosensor analysis. Kd values of tEv3 17-56 and tcEv3 16-56 dPG were 27 and 13 nM, respectively. Both compounds effectively inhibited CXCL8 induced migration of polymorphonuclear neutrophils (PMN). The present results suggest utility of synthetic Evasin-3 variants as scaffolds for designing and fine-tuning new chemokine-binding agents that suppress immune responses and inflammation. Tick saliva protein Evasin-3 modulates chemotaxis by disrupting CXCL8 interactions with glycosaminoglycans and CXCR2.,Denisov SS, Ippel JH, Heinzmann ACA, Koenen RR, Ortega-Gomez A, Soehnlein O, Hackeng TM, Dijkgraaf I J Biol Chem. 2019 Jun 24. pii: RA119.008902. doi: 10.1074/jbc.RA119.008902. PMID:31235521 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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