2lkt | pdb_00002lkt
From Proteopedia
Solution structure of N-terminal domain of human TIG3 in 2 M UREA
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Structural highlights
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.[1] Publication Abstract from PubMedHuman TIG3 protein is a member of H-REV107 protein family which belongs to the type II tumor suppressor family. TIG3 can induce apoptosis in cancer cells, and it also possesses Ca(2+)-independent phospholipase A(1/2) activity. The NMR assignments of the N-terminal domain of TIG3 are essential for its solution structure determination. (1)H, (13)C, and (15)N resonance assignments of the N-terminal domain of human TIG3.,Wang L, Yu W, Ren X, Lin J, Jin C, Xia B Biomol NMR Assign. 2012 Jan 31. PMID:22290676[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 10:12, 12 May 2021.