Biomedical subjects

P M Colman

Publications and source records attributed to P M Colman.

75 records · Page 5Linked to original sources

PubMedDate not supplied

Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution.

The influenza virus neuraminidase glycoprotein is a tetramer with a box-shaped head, 100 X 100 X 60 A, attached to a slender stalk. The three-dimensional structure of neuraminidase heads shows that each monomer is composed of six topologically identical beta-sheets arranged in a propeller formation. The tetrameric enzyme has circular 4-fold symmetry stabilized in part by metal ions bound on the symmetry axis. Sugar residues are attached to four of the five potential glycosylation sequences, and in one case contribute to the interaction between subunits in the tetramer.

Antigens, Viral↗

PubMedDate not supplied

Structure of the catalytic and antigenic sites in influenza virus neuraminidase.

The catalytic sites of influenza virus neuraminidase are located on the upper corners of the box-shaped tetramer that forms the head of the molecule. Antigenic determinants form a nearly-continuous surface across the top of the monomer encircling the catalytic site. Approximately the same number of amino acid sequence changes occurred in these determinants between the years 1968 and 1975 as occurred in the antigenic sites of influenza virus haemagglutinin in the same period.

Amino Acid Sequence↗

PubMedDate not supplied

Three-dimensional structure of a complex of antibody with influenza virus neuraminidase.

The structure of a complex between influenza virus neuraminidase and an antibody displays features inconsistent with the inflexible 'lock and key' model of antigen-antibody binding. The structure of the antigen changes on binding, and that of the antibody may also change; the interaction therefore has some of the character of a handshake.

Amino Acid Sequence↗