June Ereño-Orbea

TL;DR: An immunogen that could engage B cells from HIV-uninfected individuals that express the germline versions of the immunoglobulin genes harbored by a particular class of bNAbs is engineered, suggesting that the immunogen is a promising candidate for a human vaccine prime.

TL;DR: This review aims to provide a summary of the current knowledge on theStructural basis of ligand recognition and on the structural effects caused by these ligands in CBS domain containing proteins.

TL;DR: The authors structurally characterize the ectodomain of CD22 and present its crystal structure with the bound therapeutic antibody epratuzumab, which gives insights into the mechanism of inhibition of B-cell activation.

TL;DR: The absence of large conformational changes and the crystal structure of the partially activated pathogenic D444N mutant suggest that the rotation of CBS motifs and relaxation of loops delineating the entrance to the catalytic site represent the most likely molecular mechanism of CBS activation by S-adenosyl-l-methionine.

TL;DR: The crystal structure of an engineered human CBS construct bound to S-adenosylmethionine (AdoMet) reveals the unique binding site of the allosteric activator and the architecture of the human CBS enzyme in its activated conformation, paving the way for the rational design of compounds modulating hCBS activity and thus transsulfuration, redox status, and H2S biogenesis.