Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 16, Issue 1, Pages 89-90Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1522
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Funding
- Tsinghua University
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TNFAIP8-like 2 (TIPE2) has an essential role in immune homeostasis, yet the underlying mechanism remains enigmatic. The high-resolution crystal structure of TIPE2 reveals a previously uncharacterized fold that is different from the predicted fold of a death effector domain (DED). Strikingly, TIPE2 contains a large, hydrophobic central cavity that is poised for cofactor binding. These structural features will be important for understanding the functions of TIPE2 and other TNFAIP8 family proteins.
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