Structural highlights
Function
[TRI23_HUMAN] Acts as an E3 ubiquitin-protein ligase. In the presence of the human cytomegalovirus (HCMV) protein UL144, participates in 'Lys-63'-linked auto-ubiquitination of TRAF6 resulting in the virally controlled activation of NF-kappa-B at early time of infection. The C-terminus can act as an allosteric activator of the cholera toxin catalytic subunit.[1]
Publication Abstract from PubMed
Tripartite motif (TRIM) proteins comprise a large family of RING-type ubiquitin E3 ligases that regulate important biological processes. An emerging general model is that TRIMs form elongated antiparallel coiled-coil dimers that prevent interaction of the two attendant RING domains. The RING domains themselves bind E2 conjugating enzymes as dimers, implying that an active TRIM ligase requires higher-order oligomerization of the basal coiled-coil dimers. Here, we report crystal structures of the TRIM23 RING domain in isolation and in complex with an E2-ubiquitin conjugate. Our results indicate that TRIM23 enzymatic activity requires RING dimerization, consistent with the general model of TRIM activation.
Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase.,Dawidziak DM, Sanchez JG, Wagner JM, Ganser-Pornillos BK, Pornillos O Proteins. 2017 Jul 6. doi: 10.1002/prot.25348. PMID:28681414[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vichi A, Payne DM, Pacheco-Rodriguez G, Moss J, Vaughan M. E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1). Proc Natl Acad Sci U S A. 2005 Feb 8;102(6):1945-50. Epub 2005 Jan 31. PMID:15684077 doi:http://dx.doi.org/10.1073/pnas.0409800102
- ↑ Dawidziak DM, Sanchez JG, Wagner JM, Ganser-Pornillos BK, Pornillos O. Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase. Proteins. 2017 Jul 6. doi: 10.1002/prot.25348. PMID:28681414 doi:http://dx.doi.org/10.1002/prot.25348
