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 …
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 …
A molecular dynamics method has been developed to describe the structural and dynamic properties of protein-ligand complexes that are truncated to their active sites.
Starting from the known three-dimensional structure of the class I major histocompatibility complex-encoded HLA-B*2705 protein, three non-natural nonapeptides were designed to fit …
From the three-dimensional structure of the class I major histocompatibility complex (MHC) HLA-B*2705 protein, several nonnatural peptides were designed either to optimize the …
Truncated protein-ligand active-site complexes were studied by molecular dynamics simulations.
The class I major histocompatibility complex-encoded HLA-B*2705 protein was simulated in complex with six different peptides exhibiting unexpected structure-activity relationships.
Nicht α-helical, sondern gestreckt ist die Konformation des antigenen Peptids in der Bindungstasche des menschlichen Haupt-Histokompatibilitätskomplex-(MHC)-Proteins HLA-A2 der …
The conformation is not α-helical, but extended when the antigenic peptide binds in the pocket of the human major histocompatibility complex (MHC) protein HLA-A2 of class I.
Computer simulation of the conformations of short antigenic peptides (5–10 residues) either free or bound to their receptor, the major histocompatibility complex (MHC)-encoded …