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PDBsum entry 1nnc

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Hydrolase (o-glucosyl) PDB id
1nnc
Jmol
Contents
Protein chain
388 a.a.
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN
MAN
NAG ×2
ZMR
Metals
_CA
Waters ×197

References listed in PDB file
Key reference
Title Three-Dimensional structure of the complex of 4-Guanidino-Neu5ac2en and influenza virus neuraminidase.
Authors J.N.Varghese, V.C.Epa, P.M.Colman.
Ref. Protein Sci, 1995, 4, 1081-1087. [DOI no: 10.1002/pro.5560040606]
PubMed id 7549872
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a percentage match of 88%.
Abstract
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.
Secondary reference #1
Title Rational design of potent sialidase-Based inhibitors of influenza virus replication.
Authors M.Von itzstein, W.Y.Wu, G.B.Kok, M.S.Pegg, J.C.Dyason, B.Jin, T.Van phan, M.L.Smythe, H.F.White, S.W.Oliver.
Ref. Nature, 1993, 363, 418-423.
PubMed id 8502295
Abstract
Secondary reference #2
Title The structure of the complex between influenza virus neuraminidase and sialic acid, The viral receptor.
Authors J.N.Varghese, J.L.Mckimm-Breschkin, J.B.Caldwell, A.A.Kortt, P.M.Colman.
Ref. Proteins, 1992, 14, 327-332.
PubMed id 1438172
Abstract
Secondary reference #3
Title Refined atomic structures of n9 subtype influenza virus neuraminidase and escape mutants.
Authors W.R.Tulip, J.N.Varghese, A.T.Baker, A.Van donkelaar, W.G.Laver, R.G.Webster, P.M.Colman.
Ref. J Mol Biol, 1991, 221, 487-497.
PubMed id 1920429
Abstract
Secondary reference #4
Title Three-Dimensional structure of the neuraminidase of influenza virus a/tokyo/3/67 at 2.2 a resolution.
Authors J.N.Varghese, P.M.Colman.
Ref. J Mol Biol, 1991, 221, 473-486.
PubMed id 1920428
Abstract
Secondary reference #5
Title Three-Dimensional structure of neuraminidase of subtype n9 from an avian influenza virus.
Authors A.T.Baker, J.N.Varghese, W.G.Laver, G.M.Air, P.M.Colman.
Ref. Proteins, 1987, 2, 111-117.
PubMed id 3447170
Abstract
Secondary reference #6
Title Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 a resolution.
Authors J.N.Varghese, W.G.Laver, P.M.Colman.
Ref. Nature, 1983, 303, 35-40.
PubMed id 6843658
Abstract
PROCHECK
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