Robert G. Urban

TL;DR: A dimer of the class II αβ heterodimers is seen in the crystal forms of HLA-DR1, suggesting class II HLA dimerization as a mechanism for initiating the cytoplasmic signalling events in T-cell activation.

TL;DR: An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist, providing a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.

TL;DR: Most of the peptides derived from endogenous proteins that intersect the endocytic/class II pathway, even though class II molecules are thought to function mainly in the presentation of exogenous foreign peptide antigens, were derived from major histocompatibility complex-related molecules.

TL;DR: The characterization of acid-eluted peptides bound to HLA-DR1 by high-performance liquid chromatography, mass spectrometry and microsequencing analyses confirmed that all of the isolated peptides had high affinity for the groove of DR1.

TL;DR: The structure of a bacterial superantigen bound to a human class II histocompatibility complex molecule (HLA-DR1) has been determined by X-ray crystallography and suggests a model for ternary complex formation with the T-cell antigen receptor (TCR), in which unconventional TCR-MHC contacts are possible.