4gb1 | pdb_00004gb1

Synthesis and Evaluation of Novel 3-C-alkylated-Neu5Ac2en Derivatives as Probes of Influenza Virus Sialidase 150-loop flexibility

spinqualitylabelsall models 4gb1, resolution 2.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gb1 is a 1 chain structure with sequence from Influenza a virus (a/duck/ukraine/1/1963(h3n8)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 0LP, CA Activity: Exo-alpha-sialidase, with EC number 3.2.1.18 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Novel 3-C-alkylated-Neu5Ac2en derivatives have been designed to target the expanded active site cavity of influenza virus sialidases with an open 150-loop, currently seen in X-ray crystal structures of influenza A virus group-1 (N1, N4, N5, N8), but not group-2 (N2, N9), sialidases. The compounds show selectivity for inhibition of H5N1 and pdm09 H1N1 sialidases over an N2 sialidase, providing evidence of the relative 150-loop flexibility of these sialidases. In a complex with N8 sialidase, the C3 substituent of 3-phenylally-Neu5Ac2en occupies the 150-cavity while the central ring and the remaining substituents bind the active site as seen for the unsubstituted template. This new class of inhibitors, which can 'trap' the open 150-loop form of the sialidase, should prove useful as probes of 150-loop flexibility. Synthesis and evaluation of novel 3-C-alkylated-Neu5Ac2en derivatives as probes of influenza virus sialidase 150-loop flexibility.,Rudrawar S, Kerry PS, Rameix-Welti MA, Maggioni A, Dyason JC, Rose FJ, van der Werf S, Thomson RJ, Naffakh N, Russell RJ, von Itzstein M Org Biomol Chem. 2012 Sep 14. PMID:22976385 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Neuraminidase

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