Crystal structure of TIPE2 provides insights into immune homeostasis

Xu Zhang, Jiawei Wang, Chao Fan, Hubo Li, Honghong Sun, Shunyou Gong, Youhai H. Chen, Yigong Shi*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

101 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)89-90
Number of pages2
JournalNature Structural and Molecular Biology
Volume16
Issue number1
DOIs
StatePublished - Jan 2009

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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