Crystal structure of TIPE2 provides insights into immune homeostasis.
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.
Zhang
Xu
X
Center for Structural Biology and Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
Wang
Jiawei
J
Fan
Chao
C
Li
Hubo
H
Sun
Honghong
H
Gong
Shunyou
S
Chen
Youhai H
YH
Shi
Yigong
Y
D006706:Homeostasis; D007109:Immunity; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry* / Q000276:immunology* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D047908:Intracellular Signaling Peptides and Proteins; C529002:TIPE2 protein, mouse