Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
RNF4 [RING (really interesting new gene) finger protein 4] family ubiquitin ligases are RING E3 ligases that regulate the homoeostasis of SUMOylated proteins by promoting their ubiquitylation. In the present paper we report that the RING domain of RNF4 forms a stable dimer, and that dimerization is required for ubiquitin transfer. Our results suggest that the stability of the E2~ubiquitin thioester bond is regulated by RING domain dimerization.
RING domain dimerization is essential for RNF4 function.,Liew CW, Sun H, Hunter T, Day CL Biochem J. 2010 Oct 1;431(1):23-9. PMID:20681948[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liew CW, Sun H, Hunter T, Day CL. RING domain dimerization is essential for RNF4 function. Biochem J. 2010 Oct 1;431(1):23-9. PMID:20681948 doi:10.1042/BJ20100957
