Structure of TRAF Family: Current Understanding of Receptor Recognition

Front Immunol. 2018 Aug 30:9:1999. doi: 10.3389/fimmu.2018.01999. eCollection 2018.

Abstract

Tumor necrosis factor receptor-associated factor (TRAF) proteins are key signaling molecules that function in various cellular signaling events including immune response, cell death and survival, development, and thrombosis. Their roles in cellular signaling are mediated mostly by direct interactions with various receptors via the TRAF domain. To determine how specific TRAF domains can interact with various receptors with a limited binding interface and how similar binding interfaces of TRAF family members can recognize their specific binding partners, extensive structural studies on TRAF family proteins have been conducted for several decades. In this review, we discuss the current understanding of the structural and molecular diversity of the TRAF domain and TRAF-binding motifs in many receptors according to available structural information.

Keywords: TRAF domain; TRAF family; inflammation; innate immunity; protein interaction; structure.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Motifs / genetics
  • Animals
  • Humans
  • Immunity, Innate*
  • Inflammation / immunology*
  • Molecular Structure
  • Protein Binding
  • Protein Conformation
  • Protein Domains / genetics
  • Signal Transduction
  • Structure-Activity Relationship
  • Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / genetics
  • Tumor Necrosis Factor Receptor-Associated Peptides and Proteins / metabolism*

Substances

  • Tumor Necrosis Factor Receptor-Associated Peptides and Proteins