6I9H

Solution structure of TRIM28 RING domain

Summary for 6I9H

• Entry DOI: 10.2210/pdb6i9h/pdb
• NMR Information: BMRB: 34330
• Descriptor: Transcription intermediary factor 1-beta, ZINC ION (2 entities in total)
• Functional Keywords: trim, e3 ligase, enzyme, ubiquitin, signaling protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 9805.68

Authors

Stevens, R.V.,Esposito, D.,Rittinger, K. (deposition date: 2018-11-23, release date: 2019-05-01, Last modification date: 2024-06-19)

Primary citation

Stevens, R.V.,Esposito, D.,Rittinger, K.
Characterisation of class VI TRIM RING domains: linking RING activity to C-terminal domain identity.
Life Sci Alliance, 2:-, 2019

PubMed Abstract: TRIM E3 ubiquitin ligases regulate multiple cellular processes, and their dysfunction is linked to disease. They are characterised by a conserved N-terminal tripartite motif comprising a RING, B-box domains, and a coiled-coil region, with C-terminal domains often mediating substrate recruitment. TRIM proteins are grouped into 11 classes based on C-terminal domain identity. Class VI TRIMs, TRIM24, TRIM33, and TRIM28, have been described as transcriptional regulators, a function linked to their C-terminal plant homeodomain and bromodomain, and independent of their ubiquitination activity. It is unclear whether E3 ligase activity is regulated in family members where the C-terminal domains function independently. Here, we provide a detailed biochemical characterisation of the RING domains of class VI TRIMs and describe the solution structure of the TRIM28 RING. Our study reveals a lack of activity of the isolated RING domains, which may be linked to the absence of self-association. We propose that class VI TRIMs exist in an inactive state and require additional regulatory events to stimulate E3 ligase activity, ensuring that associated chromatin-remodelling factors are not injudiciously degraded.

PubMed: 31028095
DOI: 10.26508/lsa.201900295

Experimental method

SOLUTION NMR