Ubiquitin C-terminal Hydrolases (UCHL-1) deubiquitylating enzyme modulates the activity and localization of ubiquitin protein. UCHL-1 is highly expressed in the mammalian brain. Studies in the literature showed a point mutation at Ille93 to Met (I93M) is correlated to diseases including tumor progression, severe forms of mental retardation, and neurodegenerative disorders. However, the molecular mechanism behind Ubiquitin C-terminal Hydrolases remains unsolved. Here, we use computational chemistry methods and ab initio quantum chemistry methods to understand the molecular interactions between UCHL-1 and inhibitors (see Figure 1). We analyzed the interactions between inhibitors and UCHL-1 and identified the binding pockets. Through the analysis of electronic structures of the inhibition interactions, we propose effective ways to find better inhibitors that are testable in experiments.

Investigating the binding interactions between ubiquitin c-terminal hydrolases and inhibitors

251st National Meeting (2016)

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