5JPX

Solution structure of the TRIM21 B-box2 (B2)

Summary for 5JPX

• Entry DOI: 10.2210/pdb5jpx/pdb
• NMR Information: BMRB: 30075
• Descriptor: E3 ubiquitin-protein ligase TRIM21, ZINC ION (2 entities in total)
• Functional Keywords: b-box, metal binding protein, ring-like fold, e3 ligase, trim protein, zinc-binding motif, ubiquitination
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 5209.32

Authors

Wallenhammar, A.,Anandapadamanaban, M.,Sunnerhagen, M. (deposition date: 2016-05-04, release date: 2017-08-09, Last modification date: 2024-06-19)

Primary citation

Wallenhammar, A.,Anandapadamanaban, M.,Lemak, A.,Mirabello, C.,Lundstrom, P.,Wallner, B.,Sunnerhagen, M.
Solution NMR structure of the TRIM21 B-box2 and identification of residues involved in its interaction with the RING domain.
PLoS ONE, 12:e0181551-e0181551, 2017

PubMed Abstract: Tripartite motif-containing (TRIM) proteins are defined by the sequential arrangement of RING, B-box and coiled-coil domains (RBCC), where the B-box domain is a unique feature of the TRIM protein family. TRIM21 is an E3 ubiquitin-protein ligase implicated in innate immune signaling by acting as an autoantigen and by modifying interferon regulatory factors. Here we report the three-dimensional solution structure of the TRIM21 B-box2 domain by nuclear magnetic resonance (NMR) spectroscopy. The structure of the B-box2 domain, comprising TRIM21 residues 86-130, consists of a short α-helical segment with an N-terminal short β-strand and two anti-parallel β-strands jointly found the core, and adopts a RING-like fold. This ββαβ core largely defines the overall fold of the TRIM21 B-box2 and the coordination of one Zn2+ ion stabilizes the tertiary structure of the protein. Using NMR titration experiments, we have identified an exposed interaction surface, a novel interaction patch where the B-box2 is likely to bind the N-terminal RING domain. Our structure together with comparisons with other TRIM B-box domains jointly reveal how its different surfaces are employed for various modular interactions, and provides extended understanding of how this domain relates to flanking domains in TRIM proteins.

PubMed: 28753623
DOI: 10.1371/journal.pone.0181551

Experimental method

SOLUTION NMR