1kwe

SOLUTION STRUCTURE OF THE CENTRAL CONSERVED REGION OF HUMAN RESPIRATORY SYNCYTIAL VIRUS ATTACHMENT GLYCOPROTEIN G

spinqualitylabelsall models 1kwe Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1kwe is a 1 chain structure with sequence from Human respiratory syncytial virus A strain Long. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLYC_HRSVL Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities (By similarity). Secreted glycoprotein G helps RSV escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fcgamma receptors (By similarity). Publication Abstract from PubMed BBG2Na is a recombinant protein, composed in part of carrier protein BB and of the central conserved domain of the attachment glycoprotein G of human respiratory syncytial virus (HRSV) subgroup A. This protein is a potent vaccine candidate against HRSV. G2Na contains several contiguous B-cell epitopes, occupying sequential positions in the linear sequence of the protein. One of the epitopes contains four cysteines that are completely conserved in known strains of HRSV and form a 'cysteine noose' motif. In this study, we analysed circular dichroism (CD) spectra of BBG2Na and its B-cell epitopes. We also used NMR and molecular dynamics simulations to determine the three-dimensional structure of the cysteine noose domain. We observed significant structural differences related to the length of peptides containing the cysteine noose. These differences show good correlation with the immunogenic activity of the peptides. It is shown that a single Val(171) addition induces a pronounced structure stabilization of the cysteine noose peptide G4a (1-4/2-3) (residues 172-187), which is associated with a 100-fold increase in its antigenicity vis-a-vis a G-protein specific monoclonal antibody. Structure-antigenicity relationship studies of the central conserved region of human respiratory syncytial virus protein G.,Sugawara M, Czaplicki J, Ferrage J, Haeuw JF, Power UF, Corvaia N, Nguyen T, Beck A, Milton A J Pept Res. 2002 Nov;60(5):271-82. PMID:12383117 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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