López De Castro, J. A.

Molecular Mimicry of an HLA-B27-derived Ligand of Arthritis-linked Subtypes with Chlamydial Proteins

HLA-B27 is strongly associated with spondyloarthropathies, including ankylosing spondylitis and reactive arthritis.

Ramos, M.

• Oct 4, 2002 • 1 min read

Limited plasticity in the recognition of peptide epitope variants by an alloreactive CTL clone correlates directly with conservation of critical residues and inversely with peptide length.

Although self-restricted T cells are peptide-specific and can distinguish among closely related ligands, they have some flexibility in the recognition of sequence variants of their …

García-Peydró, M.

• Apr 1, 2000 • 1 min read

Nonapeptide Analogues Containing (R)-3-Hydroxybutanoate and β-Homoalanine Oligomers: Synthesis and Binding Affinity to a Class I Major Histocompatibility Complex Protein

Crystal structures of antigenic peptides bound to class I MHC proteins suggest that chemical modifications of the central part of the bound peptide should not alter binding …

Poenaru, S.

• Jul 1, 1999 • 1 min read

HLA-B27

Long-range effects in protein–ligand interactions mediate peptide specificity inl the human major histocompatibility antigen HLA-B27 (B*2701)

B*2701 differs from all other HLA-B27 subtypes of known peptide specificity in that, among its natural peptide ligands, arginine is not the only allowed residue at peptide position …

Krebs, S.

• Jan 1, 1999 • 1 min read

Alleles

The same natural ligand is involved in allorecognition of multiple HLA-B27 subtypes by a single T cell clone: role of peptide and the MHC molecule in alloreactivity.

The human alloreactive CTL clone 27S69, raised against B*2705, cross-reacts with B*2702 and B*2703, but not with B*2701, B*2704, B*2706, or B*2710.

Paradela, A.

• Nov 1, 1998 • 1 min read

Amino Acid Sequence

Fine specificity of antigen binding to two class I major histocompatibility proteins (B2705 and B2703) differing in a single amino acid residue.

Starting from the X-ray structure of a class I major histocompatibility complex (MHC)-encoded protein (HLA-B*2705), a naturally presented self-nonapeptide and two synthetic …

Rognan, D.

• Sep 1, 1997 • 1 min read

Molecular Mimicry of an HLA-B27-derived Ligand of Arthritis-linked Subtypes with Chlamydial Proteins

Limited plasticity in the recognition of peptide epitope variants by an alloreactive CTL clone correlates directly with conservation of critical residues and inversely with peptide length.

Nonapeptide Analogues Containing (R)-3-Hydroxybutanoate and β-Homoalanine Oligomers: Synthesis and Binding Affinity to a Class I Major Histocompatibility Complex Protein

Long-range effects in protein–ligand interactions mediate peptide specificity inl the human major histocompatibility antigen HLA-B27 (B*2701)

The same natural ligand is involved in allorecognition of multiple HLA-B27 subtypes by a single T cell clone: role of peptide and the MHC molecule in alloreactivity.

Fine specificity of antigen binding to two class I major histocompatibility proteins (B*2705 and B*2703) differing in a single amino acid residue.

Fine specificity of antigen binding to two class I major histocompatibility proteins (B2705 and B2703) differing in a single amino acid residue.