The Cusack group uses X-ray crystallography to study the structural biology of protein-RNA complexes involved in RNA metabolism, translation, RNA virus replication and innate immunity.
Aminoacyl-tRNA synthetases play an essential role in protein synthesis by charging specifically their cognate tRNA(s) with the correct amino acid. We determined the structure of cap-bound human CBC, a 90 KDa heterodimeric protein, and have studied several other proteins involved in cap-dependent processes.

A cluster of ribosomes connected by a strand of mRNA and functioning as a unit in protein synthesis.
In all eukaryotic organisms studied, this process, known as nonsense-mediated decay (NMD), crucially depends on the three conserved Upf proteins (Upf1, Upf2 and Upf3). We obtained the first structural information on binary complexes of these three proteins whose ternary complex formation triggers decay.

Another major project is innate immune pattern recognition receptors such as NOD proteins and RIG-I like helicases.

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