Structure of influenza virus haemagglutinin complexed with a neutralizing antibody
Article Abstract:
A radical change is seen in the cystallographic structure of the antigen-binding fragment (Fab) combining sites of a neutralizing antibody when it is combined with the membrane-distal domain of a hemagglutinin (HA) subunit. The research indicates that inhibition of receptor binding is one factor in infectivity neutralization. The influenza virus maintains its conserved receptor-binding site despite the immune selective pressure for change in this region of the molecule by nonessential HA residue mutations that prevent antibody binding while the receptor binding site remains unchanged. A complete description of the endosomal pH-induced fusion-active HA structure has been revealed.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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Structural basis for the regulation of tubulin by vinblastine
Article Abstract:
A report on the X-ray structure of vinblastine bound to tubulin in a complex with the RB3 protein stathmin-like domain (RB3-SLD) is presented. The results revealed that vinblastine and the amino-terminal part of RB3-SLD binding sites share a hydrophobic groove on the alpha-tubulin surface that is located at an intermolecular contact in microtubules.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain
Article Abstract:
The structure, at 3.5A resolution, of tubulin in complex with colchicines and with the stathmin-like domain (SLD) of RB3 is presented. A relationship between the onset and speed of microtube disassembly and the changes in tubulin subunits when tubulin switches from its straight to its curved conformation is established.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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