2MY9

Solution structure of N-terminal domain of human TIG3

Summary for 2MY9

• Entry DOI: 10.2210/pdb2my9/pdb
• Related: 2lkt
• NMR Information: BMRB: 25448
• Descriptor: Retinoic acid receptor responder protein 3 (1 entity in total)
• Functional Keywords: tig3, h-rev107 family, nlpc/p60, phospholipase, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Membrane ; Single-pass membrane protein : Q9UL19
• Total number of polymer chains: 1
• Total formula weight: 14050.89

Authors

Wei, H.,Wang, L.,Xia, B. (deposition date: 2015-01-21, release date: 2015-04-15, Last modification date: 2024-05-01)

Primary citation

Wei, H.,Wang, L.,Ren, X.,Yu, W.,Lin, J.,Jin, C.,Xia, B.
Structural and functional characterization of tumor suppressors TIG3 and H-REV107.
Febs Lett., 589:1179-1186, 2015

PubMed Abstract: 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.

PubMed: 25871522
DOI: 10.1016/j.febslet.2015.04.002

Experimental method

SOLUTION NMR