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Crystal structure of TIPE2 provides insights into immune homeostasis.

Authors
  • Zhang, Xu
  • Wang, Jiawei
  • Fan, Chao
  • Li, Hubo
  • Sun, Honghong
  • Gong, Shunyou
  • Chen, Youhai H
  • Shi, Yigong
Type
Published Article
Journal
Nature Structural & Molecular Biology
Publisher
Springer Nature
Publication Date
Jan 01, 2009
Volume
16
Issue
1
Pages
89–90
Identifiers
DOI: 10.1038/nsmb.1522
PMID: 19079267
Source
Medline
License
Unknown

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.

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