TRAF1 from a Structural Perspective

• Published in: Biomolecules (Basel, Switzerland) Vol. 14; no. 5; p. 510
• Main Authors: Jang, Hyunseok, Kim, Subin, Kim, Do Yeon, Han, Ju Hee, Park, Hyun Ho
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 01.05.2024
• Subjects: Amino acids; Animals; Cell fate; Cell physiology; Humans; Immune response; Kinases; Metabolism; Models, Molecular; Physiological aspects; Protein Binding; Protein Domains; protein interaction; Proteins; Roles; Signal Transduction; structure; Thrombosis; TNF Receptor-Associated Factor 1 - chemistry; TNF Receptor-Associated Factor 1 - genetics; TNF Receptor-Associated Factor 1 - metabolism; TRAF domain; TRAF1; Tumor necrosis factor; Tumor necrosis factor-TNF; South Korea; protein interaction; TRAF1; structure; TRAF domain
• ISSN: 2218-273X; 2218-273X
• DOI: 10.3390/biom14050510

Tumor necrosis factor receptor-associated factor (TRAF) proteins play pivotal roles in a multitude of cellular signaling pathways, encompassing immune response, cell fate determination, development, and thrombosis. Their involvement in these processes hinges largely on their ability to interact directly with diverse receptors via the TRAF domain. Given the limited binding interface, understanding how specific TRAF domains engage with various receptors and how structurally similar binding interfaces of TRAF family members adapt their distinct binding partners has been the subject of extensive structural investigations over several decades. This review presents an in-depth exploration of the current insights into the structural and molecular diversity exhibited by the TRAF domain and TRAF-binding motifs across a range of receptors, with a specific focus on TRAF1.