3FPT
The Crystal Structure of the Complex between Evasin-1 and CCL3
Summary for 3FPT
Entry DOI | 10.2210/pdb3fpt/pdb |
Related | 3FPU 3fpr |
Descriptor | Evasin-1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | novel fold, glycosylated protein, glycoprotein, secreted, immune system |
Biological source | Rhipicephalus sanguineus (Brown dog tick) |
Total number of polymer chains | 3 |
Total formula weight | 35246.59 |
Authors | Shaw, J.P.,Dias, J.M. (deposition date: 2009-01-06, release date: 2010-01-26, Last modification date: 2024-10-30) |
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 Cited by 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: 20041127DOI: 10.1371/journal.pone.0008514 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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