Dear Editor, TRIM proteins play important roles in a wide range of biological processes,including cell proliferation,differentiation,development,apoptosis,oncogenesis and innate immunity [1,2].The N-terminal regions of all TRIM proteins contain a RING finger domain followed by one or two B-box domains and a coiled-coil domain (CCD).The RING-finger domain comprises conserved cysteine and histidine residues that bind two zinc atoms in a ‘cross-brace' arrangement,and is essential for recruiting the ubiquitin-charged ubiquitin-conjugating enzymes (E2～Ub).The B-box domains,differing in both the number and spacing of the conserved cysteine and histidine residues [3],are typically composed of B 1 and B2 domains,but some TRIM members only contain a B2 domain.CCD following the B-box domains has been proposed to mediate protein-protein interactions,particularly homomeric and heteromeric interactions by forming intertwining helices among TRIM family and other proteins [4,5].
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