Crystal structure of TIPE2 provides insights into immune homeostasis

Nat Struct Mol Biol. 2009 Jan;16(1):89-90. doi: 10.1038/nsmb.1522. Epub 2008 Dec 14.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Homeostasis
  • Immunity*
  • Intracellular Signaling Peptides and Proteins / chemistry*
  • Intracellular Signaling Peptides and Proteins / immunology*
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary

Substances

  • Intracellular Signaling Peptides and Proteins
  • TIPE2 protein, mouse

Associated data

  • PDB/3F4M