title: Crystal structure of TIPE2 provides insights into immune homeostasis.
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.
authors.affiliation: Center for Structural Biology and Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.
authors.forename: Xu
authors.initials: X
authors.lastname: Zhang
authors.forename: Jiawei
authors.initials: J
authors.lastname: Wang
authors.forename: Chao
authors.initials: C
authors.lastname: Fan
authors.forename: Hubo
authors.initials: H
authors.lastname: Li
authors.forename: Honghong
authors.initials: H
authors.lastname: Sun
authors.forename: Shunyou
authors.initials: S
authors.lastname: Gong
authors.forename: Youhai H
authors.initials: YH
authors.lastname: Chen
authors.forename: Yigong
authors.initials: Y
authors.lastname: Shi
mesh_terms: 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
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; C529002:TIPE2 protein, mouse