The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation

• Published in: Nature (London) Vol. 353; no. 6342; pp. 321 - 325
• Main Authors: Madden, D. R, Gorga, J. C, Strominger, J. L, Wiley, D. C
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 26.09.1991; Nature Publishing Group
• Subjects: Amino Acid Sequence; Antigens; Binding Sites; Biological and medical sciences; Cellular biology; Crystallography; Electrons; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Histocompatibility antigens (hla, h-2 and other systems); HLA-B27 Antigen - chemistry; HLA-B27 Antigen - metabolism; Immunity (Disease); Medical research; Models, Molecular; Molecular immunology; Molecular Sequence Data; Molecules; Oligopeptides - metabolism; Peptides; Protein Binding; Protein Conformation; X-ray crystallography; Human; HLA-System; Peptides; Molecular structure; Major histocompatibility system; Molecular interaction; Binding site; X ray diffraction; Class I histocompatibility antigen
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/353321a0

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.