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. Author manuscript; available in PMC: 2014 Mar 1.
Published in final edited form as: Crit Rev Biochem Mol Biol. 2012 Dec 13;48(2):89–97. doi: 10.3109/10409238.2012.742856

Figure 3.

Figure 3

The linkers (in brown) in Cullin-RING E3 ligases (CRL) allosterically regulate the ubiquitination. CRL consists four components, RING-box protein (RBX, cyan), cullin (yellow), adaptor (orange), and substrate-binding protein (SBP, blue). RBX binds to E2 (green) and SBP binds to substrate protein (S, pink). Ubiquitin (Ub) is transferred from E2 to target protein. CRL works as a flexible two arm machine. RBX and SBP are the two flexible arms, and the cullin serves as the flexible scaffold. They work together to adjust the E2-ubiquitin distance for the efficient ubiquitination.