| Literature DB >> 19079267 |
Xu Zhang1, Jiawei Wang, Chao Fan, Hubo Li, Honghong Sun, Shunyou Gong, Youhai H Chen, Yigong Shi.
Abstract
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.Entities:
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Year: 2008 PMID: 19079267 DOI: 10.1038/nsmb.1522
Source DB: PubMed Journal: Nat Struct Mol Biol ISSN: 1545-9985 Impact factor: 15.369