α-helix mimicry of a β-turn11Edited by J. Wells
It is shown here that the three-dimensional arrangement of the amino acids in an RGDF β-turn (sequence involved in cell adhesion) resembles that of an α-helix with a shuffled RGDF …
It is shown here that the three-dimensional arrangement of the amino acids in an RGDF β-turn (sequence involved in cell adhesion) resembles that of an α-helix with a shuffled RGDF …
X-ray diffraction studies as well as structure-activity relationships indicate that the central part of class I major histocompatibility complex (MHC)-binding nonapeptides …
We show that the mutation of an uncharged residue far from the active site to another uncharged residue can have effects on the active site without disturbing the overall structure …
In the center of the immune system, there are major histocompatibility (MHC) protein/nonapeptide complexes which are recognized by T cell.
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 …
Abstract: The B*2710 subtype differs from the HLA-B27 prototype (B*2705) only by having Glu instead of Val at position 152, in the α2 helix of the peptide-binding site.
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 …
AbstractDue to the low effective permeabilities of peptides at many absorption sites, their structure-permeation relations are of high interest.
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 …