Crystal structure of PRY-SPRY domain of human TRIM72

Crystal structure of PRY-SPRY domain of human TRIM72
Park EYKwon OBJeong BCYi JSLee CSKo YG송현규
B30.2; gustavus; spry; TRIM21; tripartite motif; 모두원외저자-2010과제평가에반영못함.; 2E21800
Issue Date
VOL 78, NO 3, 790-795
Tripartite motif-containing (TRIM) family proteins consist of multimodular domains including a relatively conserved N-terminal RBCC domain consisting of a RING finger for E3 ubiquitin ligase activity, a zinc-bound B-box for protein–protein interaction, one or two coiledcoil domains for oligomerization, and a variable C-terminal domain. In some cases, however, TRIM proteins have a PRY-SPRY domain (PRY segment followed SPRY domain identified in a Dictyostelium discoidueum kinase splA and mammalian Ca21-release channels ryanodine receptors) at their C-terminus, which has been identified as a targeting module.1,2 More than 70 members of this family have been identified and characterized, and show a very similar domain architecture; however, their cellular functions are extremely diverse, and include roles in cell proliferation, differentiation, development, oncogenesis, apoptosis, and retroviral replication.1,2 The E3 ligase activity of several TRIM proteins has been previously demonstrated, as they usually harbor a RING domain at the N-terminal region. Each TRIM protein interacts with distinct targets, which are critical in the aforementioned cellular processes.3–8 Therefore, relatively newly and incompletely characterized C-terminal domains, including the PRY-SPRY domain, are believed to be a central mediator for selective interaction with their partners. Well-studied members of the TRIM family include the following: TRIM1, TRIM5a, TRIM19, and TRIM22, which target retroviruses and prevent their replication inside cells3,6; TRIM18/MID1 and TRIM20/pyrin, which are linked to Opitz G/BBB syndrome and familial Mediterranean fever, respectively2,9; TRIM21/Ro52, which is a major autoantigen in autoimmune diseases such as rheumatoid arthritis, systemic lupus erythematosus, and Sjo¨rgen’s syndrome10,11; and TRIM63/Murf1, TRIM55/ Murf2, TRIM41, and TRIM32, which function in muscle
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