N. G. Sgourakis

This study shows that chicken Tapasin can stabilize human HLA molecules without co-chaperones and can bind peptides, suggesting its use in engineering MHC-I ligand exchange.

This paper determines the structure of a peptide-centric Chimeric Antigen Receptor (PC-CAR) complex and identifies structural principles for antigen recognition across multiple HLA allotypes.

This paper introduces engineered MHC-I molecules with enhanced stability and peptide exchange capabilities across multiple HLA allotypes, enabling improved antigen screening and TCR analysis.

This study identifies the role of TAPBPR's 16-residue loop in promoting peptide loading on MHC-I by acting as a kinetic trap, not by competing with incoming peptides.

The paper uses RosettaMHC to model SARS-CoV-2 peptide/HLA-A02 antigens and makes the models publicly available.

This study identifies a helical capping switch in IL-2 that modulates its conformational transitions and drug interactions, providing a framework for designing precision therapeutics.

This paper identifies molecular determinants of TAPBPR chaperone interactions with MHC-I molecules, showing that conformational dynamics and disulfide bonds influence recognition and antigen repertoire selection.

This paper designs a protein family with two structurally divergent folds, showing that sequences can adopt distinct conformations under different conditions.

The paper introduces a method to produce pMHC-I tetramer libraries using TAPBPR chaperone-mediated peptide exchange, enabling high-throughput analysis of TCR repertoires and pMHC-I specificities.