Molecular basis of antigen mimicry by an anti-idiotope

Article Abstract:

The anti-idiotopic antibody E5.2 functionally mimics hen egg lysozyme (HEL) in its binding with D1.3 in that similar binding interactions occur rather than attempting an identical topological replica. The mimicry involves solvent interactions, van der Waals contacts and hydrogen bonds and most likely E5.2 could provide an internal image of HEL. This research may give some idea of how antibody complementarity determining regions mimic other molecules, especially non-proteins, without amino-acid sequence homology.

Molecular structure, Mimicry (Biology), Antigens

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Structure of the V-delta domain of a human gamma-delta T-cell antigen receptor

Article Abstract:

It is becoming increasingly clear that gamma-delta T cells have different antigen recognition needs from alpha-beta T cells. New research in this field has indicated that the V-delta domain of a major histocompatibility complex class I-reactive gamma-delta T-cell antigen receptor (TCR) has key structural elements of both TCR and immunoglobulin V regions. This research has produced the first direct evidence that gamma-delta TCRs are structurally distinct from alpha-beta TCRs.

Antigen receptors, T cell, Cell differentiation

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Crystal structure of a T-cell receptor beta-chain complexed with a superantigen

Article Abstract:

The crystal structures of T-cell receptor (TCR) beta-chain, superantigens and major histocompatibility complex (MHC) proteins reveal that superantigens displace the antigenic peptide away from the combining site of the TCR. This leads to an increase in the peptide or MHC complex-induced stimulation of the T-cells. The superantigen binding site and the peptide or MHC complex binding site of the TCR are overlapping. The crystal structure of the TCR is described using a model.

Analysis, Physiological aspects, Enterotoxins, Major histocompatibility complex, Binding sites (Biochemistry), Active sites (Biochemistry)

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