7nn9: Difference between revisions
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'''NATIVE INFLUENZA VIRUS NEURAMINIDASE SUBTYPE N9 (TERN)''' | '''NATIVE INFLUENZA VIRUS NEURAMINIDASE SUBTYPE N9 (TERN)''' | ||
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==About this Structure== | ==About this Structure== | ||
7NN9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Unidentified_influenza_virus Unidentified influenza virus]. This structure supersedes the now removed PDB entry | 7NN9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Unidentified_influenza_virus Unidentified influenza virus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2nn9 2nn9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NN9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Colman, P M.]] | [[Category: Colman, P M.]] | ||
[[Category: Varghese, J N.]] | [[Category: Varghese, J N.]] | ||
[[Category: | [[Category: Neuraminidase]] | ||
[[Category: | [[Category: Sialidase]] | ||
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Revision as of 22:46, 4 May 2008
NATIVE INFLUENZA VIRUS NEURAMINIDASE SUBTYPE N9 (TERN)
OverviewOverview
The three-dimensional X-ray structure of a complex of the potent neuraminidase inhibitor 4-guanidino-Neu5Ac2en and influenza virus neuraminidase (Subtype N9) has been obtained utilizing diffraction data to 1.8 A resolution. The interactions of the inhibitor, solvent water molecules, and the active site residues have been accurately determined. Six water molecules bound in the native structure have been displaced by the inhibitor, and the active site residues show no significant conformational changes on binding. Sialic acid, the natural substrate, binds in a half-chair conformation that is isosteric to the inhibitor. The conformation of the inhibitor in the active site of the X-ray structure concurs with that obtained by theoretical calculations and validates the structure-based design of the inhibitor. Comparison of known high-resolution structures of neuraminidase subtypes N2, N9, and B shows good structural conservation of the active site protein atoms, but the location of the water molecules in the respective active sites is less conserved. In particular, the environment of the 4-guanidino group of the inhibitor is strongly conserved and is the basis for the antiviral action of the inhibitor across all presently known influenza strains. Differences in the solvent structure in the active site may be related to variation in the affinities of inhibitors to different subtypes of neuraminidase.
About this StructureAbout this Structure
7NN9 is a Single protein structure of sequence from Unidentified influenza virus. This structure supersedes the now removed PDB entry 2nn9. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase., Varghese JN, Epa VC, Colman PM, Protein Sci. 1995 Jun;4(6):1081-7. PMID:7549872 Page seeded by OCA on Sun May 4 22:46:51 2008