Article-Journal | Chemogenomics Structural Group

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

Modeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. II. Cross-reaction between a monoclonal antibody and two αβ T cell receptors

The recombinant antibody, pSAN13.

Rognan, D.

• Jan 1, 2000 • 1 min read

Modeling the interactions of a peptide-major histocompatibility class I ligand with its receptors. I. Recognition by two αβ T cell receptors

A three-dimensional model of the complex between an Influenza Hemagglutinin peptide, Ha255−262, and its restricting element, the mouse major histocompatibility complex (MHC) class …

Rognan, D.

• Jan 1, 2000 • 1 min read

Crystallography

Predicting binding affinities of protein ligands from three-dimensional models: application to peptide binding to class I major histocompatibility proteins.

A simple and fast free energy scoring function (Fresno) has been developed to predict the binding free energy of peptides to class I major histocompatibility (MHC) proteins.

Rognan, D.

• Nov 1, 1999 • 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

Amino Acid

Solution structure of a conformationally constrained Arg-Gly-Asp-like motif inserted into the alpha/beta scaffold of leiurotoxin I.

A monoclonal antibody, AC7, directed against the RGD-binding site of the GPIIIa subunit of the platelet fibrinogen receptor, interacts with activated platelet.

Kellenberger, E.

• Mar 1, 1999 • 1 min read

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.

• Jan 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

MHC

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.

• Dec 1, 1998 • 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