Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules.
The crystal structures of major histocompatibility complex (MHC) molecules contain a groove occupied by heterogeneous material thought to represent peptides central to immune recognition, although until now relatively little characterization of the peptides has been possible. Exact information about the contents of MHC grooves is now provided. Moreover, each MHC class I allele has its individual rules to which peptides presented in the groove adhere.
Falk
K
K
Max-Planck-Institut für Biologie, Abteilung Immungenetik, Tübingen, Germany.
Rötzschke
O
O
Stevanović
S
S
Jung
G
G
Rammensee
H G
HG
D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D000939:Epitopes / Q000032:analysis / Q000235:genetics; D015683:Gene Products, gag / Q000235:genetics; D006183:H-2 Antigens / Q000235:genetics*; D006678:HIV / Q000235:genetics; D015789:HLA-A2 Antigen / Q000235:genetics; D046911:Macromolecular Substances; D008285:Major Histocompatibility Complex; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid
D000939:Epitopes; D015683:Gene Products, gag; D006183:H-2 Antigens; D015789:HLA-A2 Antigen; D046911:Macromolecular Substances; D010455:Peptides