Crystal structure of TRIM20 C-terminal coiled-coil/B30.2 fragment: implications for the recognition of higher order oligomers

• DOI: 10.1038/srep10819
• Publication Date: 2015-06-04T13:28:09Z
• Authors: Christopher Weinert; Damien Morger; Aleksandra Djekic; Markus G. Grütter; Peer R. E. Mittl
• Keywords: Linker; Trim; Coiled coil

Abstract Many tripartite motif-containing (TRIM) proteins, comprising RING-finger, B-Box and coiled-coil domains, carry additional B30.2 domains on the C-terminus of TRIM motif are considered to be pattern recognition receptors involved in detection higher order oligomers (e.g. viral capsid proteins). To investigate spatial architecture proteins we determined crystal structure TRIM20Δ413 fragment at 2.4 Å resolution. This comprises central helical scaffold (CHS) C-terminal reveals an anti-parallel arrangement CHS placing B-box 170 apart from each other. Small-angle X-ray scattering confirmed that linker between is flexible solution. The suggests interaction domain extended stretch domain, which involves residues mutated inherited disease Familial Mediterranean Fever. Dimerization by means crucial for TRIM20 bind pro-IL-1β vitro . exemplify how could binding discuss three possible models TRIM5α/HIV-1 assuming different conformations domains.