Structural studies on antibody recognition and neutralization of viruses.

The purpose of this brief review is to highlight how structural information can elucidate antibody recognition and neutralization of viruses. Studies on human rhinovirus demonstrated that antibodies need not induce conformational changes for neutralization and that viruses do not conceal receptor-binding regions from immune recognition. Ross River and Sindbis virus complexes were an early example of using antibodies to demark receptor-binding regions.

Untangling the glutamate dehydrogenase allosteric nightmare.

Glutamate dehydrogenase (GDH) is found in all living organisms, but only animal GDH is regulated by a large repertoire of metabolites. More than 50 years of research to better understand the mechanism and role of this allosteric network has been frustrated by its sheer complexity. However, recent studies have begun to tease out how and why this complex behavior evolved.

The structure of apo human glutamate dehydrogenase details subunit communication and allostery.

The structure of human glutamate dehydrogenase (GDH) has been determined in the absence of active site and regulatory ligands. Compared to the structures of bovine GDH that were complexed with coenzyme and substrate, the NAD binding domain is rotated away from the glutamate-binding domain. The electron density of this domain is more disordered the further it is from the pivot helix.