3FPR

Crystal Structure of Evasin-1

Summary for 3FPR

• Entry DOI: 10.2210/pdb3fpr/pdb
• Related: 3FPT 3FPU
• Descriptor: Evasin-1 (2 entities in total)
• Functional Keywords: novel fold, glycoprotein, secreted, immune system
• Biological source: Rhipicephalus sanguineus (Brown dog tick)
• Cellular location: Secreted (Probable): P0C8E7
• Total number of polymer chains: 2
• Total formula weight: 22612.89

Authors

Dias, J.M.,Shaw, J.P. (deposition date: 2009-01-06, release date: 2010-01-12, Last modification date: 2024-10-16)

Primary citation

Dias, J.M.,Losberger, C.,Deruaz, M.,Power, C.A.,Proudfoot, A.E.I.,Shaw, J.P.
Structural basis of chemokine sequestration by a tick chemokine binding protein: the crystal structure of the complex between Evasin-1 and CCL3
Plos One, 4:-, 2009

PubMed Abstract: Chemokines are a subset of cytokines responsible for controlling the cellular migration of inflammatory cells through interaction with seven transmembrane G protein-coupled receptors. The blocking of a chemokine-receptor interaction results in a reduced inflammatory response, and represents a possible anti-inflammatory strategy, a strategy that is already employed by some virus and parasites. Anti-chemokine activity has been described in the extracts of tick salivary glands, and we have recently described the cloning and characterization of such chemokine binding proteins from the salivary glands, which we have named Evasins.

PubMed: 20041127
DOI: 10.1371/journal.pone.0008514

Experimental method

X-RAY DIFFRACTION (1.63 Å)