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Exploration of the P6/P7 region of the peptide-binding site of the human class II major histocompatability complex protein HLA-DR1.
Antagonism of HIV-specific CD4+ T cells by C-terminal truncation of a minimum epitope.
Major histocompatibility complex and T cell interactions of a universal T cell epitope from Plasmodium falciparum circumsporozoite protein.
HLA-DR: molecular insights and vaccine design.
Pseudo-merohedral twinning and noncrystallographic symmetry in orthorhombic crystals of SIVmac239 Nef core domain bound to different-length TCRzeta fragments.
A role for differential variable gene pairing in creating T cell receptors specific for unique major histocompatibility ligands.
Mapping the HLA-DO/HLA-DM complex by FRET and mutagenesis.
Antigenic peptide trimming by ER aminopeptidases--insights from structural studies.
Induced fit of an epitope peptide to a monoclonal antibody probed with a novel parallel surface plasmon resonance assay.
Probing the ligand-induced conformational change in HLA-DR1 by selective chemical modification and mass spectrometric mapping.
Fluorogenic probes for monitoring peptide binding to class II MHC proteins in living cells.
Crystallographic structure of the human leukocyte antigen DRA, DRB3*0101: models of a directional alloimmune response and autoimmunity.
Model for the peptide-free conformation of class II MHC proteins.
Conformational lability in the class II MHC 310 helix and adjacent extended strand dictate HLA-DM susceptibility and peptide exchange.
Minimal conformational plasticity enables TCR cross-reactivity to different MHC class II heterodimers.
Conformational variation in structures of classical and non-classical MHCII proteins and functional implications.
HLA-DM and HLA-DO, key regulators of MHC-II processing and presentation.
Susceptibility to HLA-DM protein is determined by a dynamic conformation of major histocompatibility complex class II molecule bound with peptide.
Broad TCR repertoire and diverse structural solutions for recognition of an immunodominant CD8+ T cell epitope.
The N-terminal region of photocleavable peptides that bind HLA-DR1 determines the kinetics of fragment release.