The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation.
X-ray crystallography reveals electron density in the antigen-binding site of HLA-B27 that is an interpretable image of nonameric peptides in a largely extended conformation. Clear density exists for the main chain and several side chains and is consistent with the sequence of 11 nonameric self-peptides eluted from HLA-B27. Pockets in the antigen-binding cleft bind four side chains and the amino and carboxyl termini of the peptide.
Committee on Higher Degrees in Biophysics, Harvard University, Cambridge, Massachusetts.
D R
DR
Madden
J C
JC
Gorga
J L
JL
Strominger
D C
DC
Wiley
D000595:Amino Acid Sequence; D001665:Binding Sites; D004583:Electrons; D015796:HLA-B27 Antigen / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation
D015796:HLA-B27 Antigen; D009842:Oligopeptides