Design of the Ligase System


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As a leading service provider in drug discovery and research, BOC Sciences is fully capable and committed to providing one-stop proteolysis targeting molecular drug discovery based on chimeric (PROTAC). With a comprehensive and advanced platform, we provides PROTAC ligase system design services to customers around the world to meet new drug discovery goals.

Introduction

Ubiquitin ligase, also known as E3 ubiquitin ligase, is an enzyme that connects ubiquitin molecules to a lysine of the target protein. E3 ligases number in the thousands and have the highest level of specificity for the target protein to be modified by ubiquitin or ubiquitin-like modifiers (UBL). In general, ubiquitin ligase can make the target protein multi-ubiquitin, which add multiple ubiquitin molecules to form a multi-ubiquitin chain, while the protein with multi-ubiquitin chain can be recognized by proteasome and degraded. However, in some cases, ubiquitin ligase connects only one ubiquitin molecule to the target protein; this mono-ubiquitin protein is not degraded by proteasome, but its location or function in cells may change; for example, mono-ubiquitin proteins can change their position by binding to other proteins with ubiquitin-binding domains.

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References:

  1. Hershko, A., Heller, H., Elias, S., & Ciechanover, A. (1983). Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. Journal of Biological Chemistry, 258(13), 8206-8214.
  2. Qian, S. B., Waldron, L., Choudhary, N., Klevit, R. E., Chazin, W. J., & Patterson, C. (2009). Engineering a ubiquitin ligase reveals conformational flexibility required for ubiquitin transfer. Journal of Biological Chemistry, 284(39), 26797-26802.

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