Peptide motifs of closely related HLA class I molecules encompass substantial differences

Tools

Item Type:	Article
Title:	Peptide motifs of closely related HLA class I molecules encompass substantial differences
Creators Name:	Roetzschke, O., Falk, K., Stevanovic, S., Jung, G. and Rammensee, H.G.
Abstract:	The peptides presented by major histocompatibility complex class I molecules adhere to strict rules concerning peptide length and occupancy by certain amino acid residues at anchor positions. Peptides presented by HLA-A0201 molecules, for example, are generally nonapeptides requiring Leu or Met at position 2 and an aliphatic residue, predominantly Val, at position 9. A closely related molecule, HLA-A0205, differing from the former at four amino acid residues, has a related but substantially different peptide motif. A0205-presented peptides are still nonapeptides, and position 9 is still aliphatic, although it is preferentially occupied by Leu instead of Val. Position 2 not only allows aliphatic residues but also polar ones. Occupancy at position 6, considered as an auxiliary anchor in A0201, as well as non-anchor residues at positions 3, 4, and 8 are relatively well conserved between the two peptide motifs. Thus, although a number of the T cell epitopes presented by the two HLA-A2 forms is expected to be identical, a considerable number of epitopes should be different.
Keywords:	Amino Acid Sequence, HLA-A Antigens, Molecular Sequence Data
Source:	European Journal of Immunology
ISSN:	0014-2980
Publisher:	Wiley
Volume:	22
Number:	9
Page Range:	2453-2456
Date:	1 September 1992
Official Publication:	https://doi.org/10.1002/eji.1830220940
PubMed:	View item in PubMed

Repository Staff Only: item control page