Post-translational modifications (PTMs) are important biological process related to numerous cellular molecular events such as cell division, signaling and protein turnover. Ubiquitination is one of the post-translational modifications which employs a 76-residue small protein called ubiquitin to modify substrate proteins. Nearly half of human proteins are involved in the ubiquitination proteasome system and (mis-)regulated ubiquitinations are frequently correlated with human diseases. My research focuses on the molecular mechanism of HERC5 E3-mediated ubiquitination in innate immune responses. HERC5 utilizes a ubiquitin-like molecular called ISG15 to modify and promote degradation of viral or bacterial proteins as an important defending responses.
To fully unveil the HERC5-mediated innate immune response, structural biology provides great tools to discover details of protein-protein interactions. I will combine solution nuclear magnetic resonance (NMR) X-ray crystallography and cryo-electron micropscopy (cryoEM) to characterize dynamic and transient reactions, allosteric activation and complex structures. The outcome will provide chances in advanced drug design for antiviral response.