4ZKQ
Viral chemokine binding protein R17 encoded by rodent gammaherpesvirus Peru ( RHVP)
Summary for 4ZKQ
| Entry DOI | 10.2210/pdb4zkq/pdb |
| Descriptor | Putative uncharacterized protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | chemokine binding protein, viral protein |
| Biological source | Cricetid herpesvirus 2 |
| Total number of polymer chains | 1 |
| Total formula weight | 47897.38 |
| Authors | Lubman, O.Y.,Fremont, D.H. (deposition date: 2015-04-30, release date: 2015-11-18, Last modification date: 2024-10-23) |
| Primary citation | Lubman, O.Y.,Fremont, D.H. Parallel Evolution of Chemokine Binding by Structurally Related Herpesvirus Decoy Receptors. Structure, 24:57-69, 2016 Cited by PubMed Abstract: A wide variety of pathogens targets chemokine signaling networks in order to disrupt host immune surveillance and defense. Here, we report a structural and mutational analysis of rodent herpesvirus Peru encoded R17, a potent chemokine inhibitor that sequesters CC and C chemokines with high affinity. R17 consists of a pair of β-sandwich domains linked together by a bridging sheet, which form an acidic binding cleft for the chemokine CCL3 on the opposite face of a basic surface cluster that binds glycosaminoglycans. R17 promiscuously engages chemokines primarily through the same N-loop determinants used for host receptor recognition while residues located in the chemokine 40s loop drive kinetically stable complex formation. The core fold adopted by R17 is unexpectedly similar to that of the M3 chemokine decoy receptor encoded by MHV-68, although, strikingly, neither the location of ligand engagement nor the stoichiometry of binding is conserved, suggesting that their functions evolved independently. PubMed: 26671708DOI: 10.1016/j.str.2015.10.018 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.898 Å) |
Structure validation
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