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Andrew J. Beavil
Researcher at King's College London
Publications - 80
Citations - 3605
Andrew J. Beavil is an academic researcher from King's College London. The author has contributed to research in topics: Immunoglobulin E & Antibody. The author has an hindex of 28, co-authored 75 publications receiving 3289 citations. Previous affiliations of Andrew J. Beavil include Randall Division of Cell and Molecular Biophysics & Medical Research Council.
Papers
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Journal ArticleDOI
The biology of IGE and the basis of allergic disease.
Hannah J. Gould,Brian J. Sutton,Andrew J. Beavil,Rebecca L. Beavil,Natalie McCloskey,Heather A. Coker,David J. Fear,Lyn Smurthwaite +7 more
TL;DR: There is now compelling evidence that the microenvironment of mucosal tissues of allergic disease favors class switching to IgE; and the exceptionally high affinity of IgE for FcepsilonRI can now be interpreted in terms of the recently determined crystal structures of IgG-FcgammaR complexes.
Journal ArticleDOI
Molecular model of a lattice of signalling proteins involved in bacterial chemotaxis
Thomas S. Shimizu,Nicolas Le Novère,Matthew D. Levin,Andrew J. Beavil,Brian J. Sutton,Dennis Bray +5 more
TL;DR: The proposed structure is a regular two-dimensional lattice in which the cytoplasmic ends of chemotactic-receptor dimers are inserted into a hexagonal array of CheA and CheW molecules, which creates separate compartments for adaptation and downstream signalling, and indicates a possible basis for the spread of activity within the cluster.
Journal ArticleDOI
Identification of Contact Residues and Definition of the CAR-Binding Site of Adenovirus Type 5 Fiber Protein
Ian Kirby,Elizabeth Davison,Andrew J. Beavil,Cecilia P. C. Soh,Thomas J. Wickham,Peter W. Roelvink,Imre Kovesdi,Brian J. Sutton,George Santis +8 more
TL;DR: Analysis of the kinetics of binding of Ad type 5 (Ad5) fiber knob to the soluble extracellular domains of CAR together and each immunoglobulin (Ig) domain independently by surface plasmon resonance demonstrated that the IgV domain is necessary and sufficient for binding, and no additional membrane components are required to confer high-affinity binding to Ad5 fiber knob.
Journal ArticleDOI
The crystal structure of IgE Fc reveals an asymmetrically bent conformation
Tommy Wan,Rebecca L. Beavil,Stella M. Fabiane,Andrew J. Beavil,Maninder K. Sohi,Maura B. Keown,Robert J. Young,Alistair James Henry,Raymond J. Owens,Hannah J. Gould,Brian J. Sutton +10 more
TL;DR: The distinguishing structural feature of immunoglobulin E (IgE), the antibody responsible for allergic hypersensitivity, is the Cε2 domain pair that replaces the hinge region of IgG, and the crystal structure of the IgE Fc at a 2.6-Å resolution has revealed these domains.
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Alpha-helical coiled-coil stalks in the low-affinity receptor for IgE (Fc epsilon RII/CD23) and related C-type lectins.
TL;DR: It appears that within the C-type lectin superfamily, there is a subfamily of structurally related membrane-bound receptor proteins that contain alpha-helical coiled-coil stalks of various lengths.