Krebs, S.

Structure-Based Design of Nonnatural Ligands for the HLA-B27 Protein

X-ray studies as well as structure-activity relationships indicate that the central part of class I MHC-binding nonapeptides represents the main interaction site for a T cell …

Deadier, S.

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.

From peptides to peptidomimetics: design of nonpeptide ligands for major histocompatibility proteins

The ever increasing data available on antigen presentation by class I or class II histocompatibility proteins have made these glycoproteins highly interesting pharmaceutical …

Krebs, S.

Substituting nonpeptidic spacers for the T cell receptor-binding part of class I major histocompatibility complex-binding peptides.

X-ray diffraction studies as well as structure-activity relationships indicate that the central part of class I major histocompatibility complex (MHC)-binding nonapeptides …

Krebs, S.

Binding of rationally designed non-natural peptides to the human leukocyte antigen HLA-B*2705

High-affinity ligands of non-peptidic nature, binding to the class I major histocompatibility complex protein HLA B*2705 whose expression is strongly linked to the pathogenesis of …

Krebs, S.

Fine specificity of antigen binding to two class I major histocompatibility proteins (B*2705 and B*2703) 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.