Amino acid sequence of an immunoglobulin-like HLA antigen heavy chain domain.

AUTOR(ES)

Trägärdh, L

RESUMO

The classical human transplantation antigens, derived from the HLA-A, -B, and -C loci, are cell-surface-expressed glycoproteins. On the exterior of the cell the transplantation antigen heavy chain exposes two disulfide-containing domains and a glycosylated NH2-terminal extension. The disulfide-containing domain closest to the membrane has been isolated and its amino acid sequence has been determined. The HLA antigens used for the sequence analysis were derived from two and possibly three loci and comprised several allelic forms. The primary structure was remarkably invariant, and amino acid variations were observed only at three positions. Whether this suggests that the allelic variation of the HLA antigens is preferentially confined to other regions of the molecule or is a result of fortuitous selection of peptides remains to be established. The sequenced portion of the HLA antigen heavy chain is as homologous to beta 2-microglobulin and immunoglobulin light and heavy chains as are the latter to one another. This observation strengthens the notion that the transplantation antigens and the immunoglobulins are evolutionarily related.

Documentos Relacionados

• An immunoglobulin-like domain determines the specificity of neurotrophin receptors.
• Multiple-alphabet amino acid sequence comparisons of the immunoglobulin kappa-chain constant domain.
• Molecular basis of two subfamilies of immunoglobulin-like chaperones.
• Activation of human eosinophils through leukocyte immunoglobulin-like receptor 7
• The HLA-DQ beta gene upstream region contains an immunoglobulin-like octamer motif that binds cell-type specific nuclear factors.