Tissue Antigens · 1998 · 26 citations · 17 references
Life SciencesGeneticsImmunologyClinical ImmunologyImmunogeneticsMolecular ImmunologyHla MatchingHla TypingHumoral ImmunityMajor Histocompatibility ComplexAntibodiesClass I Hla AntibodiesHla Class I MatchingHla Class I MoleculesHla Class I TypingHla ImmunogeneticsHuman Leukocyte Antigen B27
We report the complete coding sequence of a new HLA-B27 subtype, B*2712, which was found in a Caucasian Spanish family within the chromosome A2-Cw2-B*2712-DR15-DQ6. B*2712 was first detected as a segregating B blank Bw6-associated antigen. Extensive serologic analysis demonstrated that this new B27 subtype was not recognised by any of the B27-monospecific antibodies, giving positive reactions only with some monoclonal reagents against B40 or B27,40. Sequencing analysis showed a high similarity with B*2708, only differing in three clustered amino acid residues at positions 69 to 71 located in the alpha helix of the alpha1 domain. Residues 69 and 71 point towards the T-cell receptor, while amino acid 70 points to the antigen binding site. Loss of the conserved structure of pocket B as well as the differentiated pocket F configuration suggests that B*2712 does not confer ankylosing spondylitis susceptibility. Misleading serologic definition supports the usefulness of DNA-typing methods to complement HLA class I typing.
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Identification of self peptides bound to purified HLA-B27
Theodore S. Jardetzky, W S Lane, Ruth A. Robinson et al. · Nature · 1991 · 832 citations
The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation
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Life Sciences, Genetics, Immunology +14