Immunoglobulin A (IgA) plays a key role in defending mucosal surfaces against attack by
infectious microorganisms. Such sites present a major site of susceptibility due to their vast …

The four distinct T-cell antigen receptor polypeptides (α, β, γ, δ) form two different
heterodimers (α: β and γ: δ) that are very similar to immunoglobulins in primary sequence …

We have analysed the atomic structures of Fab and VL fragments of immunoglobulins to
determine the relationship between their amino acid sequences and the three-dimensional …

On the basis of comparative studies of known antibody structures and sequences it has
been argued that there is a small repertoire of main-chain conformations for at least five of …

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A comparative analysis of the main-chain conformation of the L1, L2, L3, H1 and H2
hypervariable regions in 17 immunoglobulin structures that have been accurately …

The three-dimensional structure of the human histocompatibility antigen HLA-A2 was
determined at 3.5 Å resolution by a combination of isomorphous replacement and iterative …

The structure of an intact, anti-canine lymphoma monoclonal antibody (Mab231) 1 was
determined by molecular replacement and refined in a triclinic cell to an R-value of 20.9 …

Fifty-one examples of oligopeptides linking protein domains were extracted from the
Brookhaven database of three-dimensional protein structures. In general, the peptides …

Do antibody combining sites possess general properties that enable them to bind different
antigens with varying affinities and to bind novel antigens? Here, we address this question …