1NCB Hydrolase(O-Glycosyl) date Jan 21, 1992
title Crystal Structures Of Two Mutant Neuraminidase-Antibody Complexes With Amino Acid Substitutions In The Interface
authors W.R.Tulip, J.N.Varghese, P.M.Colman
compound source
Molecule: Influenza A Subtype N9 Neuraminidase
Chain: N
Ec: 3.2.1.18
Organism_scientific: Influenza A Virus (Aternaustraliag70c1975(H11n9));
Organism_taxid: 384509
Strain: (Aternaustraliag70c1975(H11n9))

Molecule: Igg2a-Kappa Nc41 Fab (Light Chain)
Chain: L

Organism_scientific: Mus Musculus
Organism_common: House Mouse
Organism_taxid: 10090

Molecule: Igg2a-Kappa Nc41 Fab (Heavy Chain)
Chain: H

Organism_scientific: Mus Musculus
Organism_common: House Mouse
Organism_taxid: 10090
symmetry Space Group: P 4 21 2
R_factor 0.165 R_Free NULL
crystal
cell
length a length b length c angle alpha angle beta angle gamma
167.000 167.000 124.000 90.00 90.00 90.00
method X-Ray Diffractionresolution 2 Å
ligand BMA, CA, MAN, NAG enzyme Exo-alpha-sialidase;. Neuraminidase;. Sialidase;. Alpha-neuraminidase;. Acetylneuraminidase. Hydrolase E.C.3.2.1.18 BRENDA
related structures by homologous chain: 1IGJ, 1IKF, 1INY, 1IQW, 1NCA
domain The transmembrane domain also plays a role in lipid raft association (by similarity). Intact n-terminus is essential for virion morphogenesis. Possess two apical sorting signals, one in the ectodomain, which is likely to be a glycan, and the other in the transmembrane domain.
similarity Belongs to the glycosyl hydrolase 34 family.[Neur]
subunit Homotetramer (by similarity).
catalytic activ. Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
post-translat. modifications N-glycosylated (by similarity).
subcellular loc. Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. Type ii membrane protein. In the virion, forms a mushroom-shaped spike on the surface of the membrane (by similarity).
enzyme regulation These drugs interfere with the release of progeny virus from infected cells and are effective against all influenza strains. Inhibited by the neuraminidase inhibitors zanamivir (relenza) and oseltamivir (tamiflu). Resistance to neuraminidase inhibitors is quite rare.
Gene IGH-1A (M. musculus); NA (M. musculus)
function Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. Otherwise, infection would be limited to one round of replication. Cleaves off the terminal sialic acids on the glycosylated ha during virus budding to facilitate virus release. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication. May additionally display a raft-association independent effect on budding.
Gene
Ontology
ChainFunctionProcessComponent
H
  • antigen binding
  • antibody-dependent cellular ...
  • positive regulation of type ...
  • positive regulation of type ...
  • humoral immune response medi...
  • phagocytosis, recognition
  • phagocytosis, engulfment
  • complement activation, class...
  • endosome to lysosome transpo...
  • immunoglobulin mediated immu...
  • antigen processing and prese...
  • regulation of proteolysis
  • early endosome to late endos...
  • positive regulation of endoc...
  • positive regulation of phago...
  • positive regulation of immun...
  • positive regulation of B cel...
  • multivesicular body
  • plasma membrane
  • membrane
  • integral to membrane
  • immunoglobulin complex, circ...
  • N
  • exo-alpha-sialidase activity...
  • calcium ion binding
  • hydrolase activity
  • hydrolase activity, acting o...
  • metal ion binding
  • carbohydrate metabolic proce...
  • metabolic process
  • plasma membrane
  • membrane
  • integral to membrane
  • virion
  • host cell plasma membrane
  • virion membrane
  • Primary referenceCrystal structures of two mutant neuraminidase-antibody complexes with amino acid substitutions in the interface., Tulip WR, Varghese JN, Webster RG, Laver WG, Colman PM, J Mol Biol 1992 Sep 5;227(1):149-59. PMID:1522584
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (142 Kb) [Save to disk]
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  • Classification of representative domains in scop (Structural Classification of Proteins)
        - Domain d1ncbh1, region H:1-113 [Jmol] [rasmolscript] [script source]
        - Domain d1ncbh2, region H:114-227 [Jmol] [rasmolscript] [script source]
        - Domain d1ncbl1, region L:1-108 [Jmol] [rasmolscript] [script source]
        - Domain d1ncbl2, region L:109-214 [Jmol] [rasmolscript] [script source]
        - Domain d1ncbn_, region N [Jmol] [rasmolscript] [script source]
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