3W09
Influenza virus neuraminidase subtype N9 (TERN) complexed with 2,3-dif guanidino-neu5ac2en inhibitor
Summary for 3W09
| Entry DOI | 10.2210/pdb3w09/pdb |
| Related | 1NNC 7NN9 |
| Descriptor | Neuraminidase, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| Functional Keywords | neuraminidase, sialidase, hydrolase(o-glucosyl), hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Influenza A virus |
| Cellular location | Virion membrane (By similarity): P03472 |
| Total number of polymer chains | 1 |
| Total formula weight | 46963.80 |
| Authors | Streltsov, V.A. (deposition date: 2012-10-25, release date: 2013-05-01, Last modification date: 2024-10-16) |
| Primary citation | Kim, J.-H.,Resende, R.,Wennekes, T.,Chen, H.M.,Bance, N.,Buchini, S.,Watts, A.G.,Pilling, P.,Streltsov, V.A.,Petric, M.,Liggins, R.,Barrett, S.,McKimm-Breschkin, J.L.,Niikura, M.,Withers, S.G. Mechanism-based covalent neuraminidase inhibitors with broad-spectrum influenza antiviral activity Science, 340:71-75, 2013 Cited by PubMed Abstract: Influenza antiviral agents play important roles in modulating disease severity and in controlling pandemics while vaccines are prepared, but the development of resistance to agents like the commonly used neuraminidase inhibitor oseltamivir may limit their future utility. We report here on a new class of specific, mechanism-based anti-influenza drugs that function through the formation of a stabilized covalent intermediate in the influenza neuraminidase enzyme, and we confirm this mode of action with structural and mechanistic studies. These compounds function in cell-based assays and in animal models, with efficacies comparable to that of the neuraminidase inhibitor zanamivir and with broad-spectrum activity against drug-resistant strains in vitro. The similarity of their structure to that of the natural substrate and their mechanism-based design make these attractive antiviral candidates. PubMed: 23429702DOI: 10.1126/science.1232552 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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