Interferon-induced protein with tetratricopeptide repeats 5 (IFIT5)

Interferon-induced protein with tetratricopeptide repeats 5 (IFIT5) is an interferon-stimulated gene product with a protein size of approximately 58 kDa. It belongs to the IFIT family of RNA-binding proteins and contains multiple tetratricopeptide repeats (TPR), which form a unique clamp-like structure that enables selective binding to distinct RNA species, especially those with 5′-triphosphate or monophosphate ends, as found in viral RNAs or certain cellular transcripts[3][5]. IFIT5 plays a crucial role in innate immunity by recognizing and sequestering non-self RNA and is involved in the degradation of specific microRNAs through recruitment of exoribonuclease XRN1[4]. Beyond antiviral defense, IFIT5 has been implicated in the regulation of cancer cell migration and epithelial-mesenchymal transition, with overexpression promoting aggressive cancer phenotypes[4]. Structural studies reveal IFIT5 has a highly specialized cavity for RNA binding and undergoes notable conformational changes upon ligand interaction[3][1]. No approved drugs directly target IFIT5, but its biological significance in host defense and cancer underscores therapeutic interest.

Other names

ISG58RI58IFIT-5P58Retinoic acid- and interferon-inducible 58 kDa proteinInterferon-induced 58 kDa proteinretinoic acid- and interferon-inducible protein (58kD)

RNA recognition and sequestration, modulation of RNA processing, possible recruitment of exoribonuclease XRN1 for degradation of specific microRNAs[4]