2my9 | pdb_00002my9

Solution structure of N-terminal domain of human TIG3

spinqualitylabelsall models 2my9, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2my9 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2lkt Gene: RARRES3, RIG1, TIG3 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [HRSL4_HUMAN] Exhibits PLA1/2 activity, catalyzing the calcium-independent hydrolysis of acyl groups in various phosphotidylcholines (PC) and phosphatidylethanolamine (PE). For most substrates, PLA1 activity is much higher than PLA2 activity. N- and O-acylation activity is hardly detectable. Publication Abstract from PubMed H-REV107-like family proteins TIG3 and H-REV107 are class II tumor suppressors. Here we report that the C-terminal domains (CTDs) of TIG3 and H-REV107 can induce HeLa cell death independently. The N-terminal domain (NTD) of TIG3 enhances the cell death inducing ability of CTD, while NTD of H-REV107 plays an inhibitory role. The solution structure of TIG3 NTD is very similar to that of H-REV107 in overall fold. However, the CTD binding regions on NTD are different between TIG3 and H-REV107, which may explain their functional difference. As a result, the flexible main loop of H-REV107, but not that of TIG3, is critical for its NTD to modulate its CTD in inducing cell death. Structural and functional characterization of tumor suppressors TIG3 and H-REV107.,Wei H, Wang L, Ren X, Yu W, Lin J, Jin C, Xia B FEBS Lett. 2015 May 8;589(11):1179-86. doi: 10.1016/j.febslet.2015.04.002. Epub, 2015 Apr 11. PMID:25871522 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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