Crystal structure and nucleotide selectivity of human IFIT5/ISG58

• 作者: Christopher Crowley Feng Feng Jingjing Li Lingmin Yuan YaoE Wang Yingfang Liu Zongyang Lv
• 来源期刊: 细胞研究（英文版）
• 年，卷（期）: 2013,（8）
• 所属期刊栏目: LETTERS TO THE EDITOR
• 页码范围: 1055-1058
• 页数: 4页
• 语种: 英文
• DOI: 10.1038/cr.2013.80

摘要

Dear editor, Interferon-stimulated gene 56 (ISG56) family members,ISG56,ISG54,ISG58 and ISG60,also known as interferon-induced protein with tetratricopeptide repeats (TPR) 1 (IFIT1),IFIT2,IFIT5 and IFIT3,respectively,play crucial roles in human antiviral defense systems.Recent studies have shown that ISG56 specifically recognizes viral 5'-pppRNA [1].Using structural biology methods,we found that ISG54 possesses a right-handed helical channel in its C-terminal region,which recognizes AU-rich RNAs [2].ISG54 mutants whose nucleotidebinding sites were destroyed showed a significant loss of their antiviral activities [2].As the expression patterns of ISG56 family proteins have been reported to be cell-and inducer-specific [3],we hypothesize that different ISG56 family members likely recognize distinct substrates.