Linking Ubiquitin Research to Drug Discovery

E3 ligases confer specificity to the ubiquitylation pathway by recognising target substrates and mediating transfer of ubiquitin or ubiquitin like modifiers (UBLs) from an E2 conjugating enzyme to a substrate. There are estimated to be >700 E3 ligases forming several classes of enzyme; N-end rule ubiquitin E3 ligases, Homology to E6AP C-Terminus (HECT) domain E3s, Really Interesting New Gene (RING) domain E3s, U-Box containing E3s, Inhibitor of Apoptosis (IAP) E3s, and Cullin-RING E3 ligases (CRLs). The classes of E3 ligases are continually expanding. HECT E3 ligases form a thioester intermediate with the C-terminus of activated ubiquitin via a catalytic cysteine residue on the E3. In this case, ubiquitin is transferred from an E2 via the E3 to a substrate protein lysine side chain. RING and U-Box E3 ligases do not possess a catalytic cysteine residue and bring the E2-ubiquitin complex and substrate into close proximity to mediate the transfer of the ubiquitin directly from the E2 to the substrate.

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