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 …

This review examines protein complexes in the Brookhaven Protein Databank to gain a
better understanding of the principles governing the interactions involved in protein-protein …

A strategy, called alanine-scanning mutagenesis, was used to identify specific side chains in
human growth hormone (hGH) that strongly modulate binding to the hGH receptor cloned …

IN antibodies, a heavy and a light chain variable domain, VH and VL, respectively, pack
together and the hypervariable loops on each domain contribute to binding antigen1–4. We …

The non-covalent assembly of proteins that fold separately is central to many biological
processes, and differs from the permanent macromolecular assembly of protein subunits in …

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 …

Hepatitis C virus (HCV), a Hepacivirus, is a major cause of viral hepatitis, liver cirrhosis, and
hepatocellular carcinoma. HCV envelope glycoproteins E1 and E2 mediate fusion and entry …

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The three-dimensional structures of influenza virus haemagglutinins complexed with cell
receptor analogues show sialic acids bound to a pocket of conserved amino acids …

It is proposed to reduce the immunogenicity of allogeneic antibody variable domains, while
preserving ligand-binding properties, by reducing their antigenicity through replacement of …