3q3x | pdb_00003q3x

Crystal structure of the main protease (3C) from human enterovirus B EV93

spinqualitylabelsall models 3q3x, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3q3x is a 2 chain structure with sequence from Enterovirus B. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: GOL, MG, OCS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5DSM6_9ENTO Publication Abstract from PubMed The Enteroviruses genus of the Picornaviridae family is abundant with common human pathogens that belong to rhinoviruses (HRVs) and enteroviruses (EVs), including diverse echo-, coxsackie- and polio- viruses. They cause a wide spectrum of clinical manifestations ranging from asymptomatic to severe diseases with neurological and/or cardiac manifestations. Pandemic outbreaks of EVs may be accompanied with meningitis and/or paralysis and can be fatal. However, there is no effective prophylaxis or antiviral treatment available against most EVs. The EV RNA genome directs the synthesis of a single polyprotein that is auto-catalytically processed into mature proteins by the 3C protease at Gln downward arrowGly sites, with narrow conserved substrate specificity. These cleavages are essential for virus replication, making 3C(pro) an excellent target for antivirus drug development. In this study, we report the first crystal structures of the 3C(pro) from an enterovirus B, EV-93, a recently identified pathogen, alone and in complex with the anti-HRV molecules Compound 1 (AG7404) and Rupintrivir (AG7088), at 1.9, 1.3 and 1.5-A resolution, respectively. The EV-93 3C(pro) adopts a chymotrypsin-like fold with a canonically configured oxyanion hole and a substrate binding pocket similar to that of rhino-, coxsackie- and poliovirus 3C proteases. We show that Compound 1 and Rupintrivir are both active against EV-93 in infected cells, and inhibit the proteolytic activity of EV-93 3C(pro) in vitro. These results provide a framework for further structure-guided optimization of the tested compounds to produce antiviral drugs against a broad range of EV species. Structural basis for antiviral inhibition of the main protease 3C from human enterovirus 93.,Costenaro L, Kaczmarska Z, Arnan C, Janowski R, Coutard B, Sola M, Gorbalenya AE, Norder H, Canard B, Coll M J Virol. 2011 Aug 10. PMID:21835784 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus protease 3D structures

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