Structural basis of RNA recognition and activation by innate immune receptor RIG-I

被引：0
作者：
Fuguo Jiang
Anand Ramanathan
Matthew T. Miller
Guo-Qing Tang
Michael Gale
Smita S. Patel
Joseph Marcotrigiano
机构：
[1] Center for Advanced Biotechnology and Medicine,Department of Chemistry and Chemical Biology
[2] Rutgers University,Department of Biochemistry
[3] 679 Hoes Lane West,Department of Immunology
[4] Piscataway,undefined
[5] New Jersey 08854,undefined
[6] USA,undefined
[7] UMDNJ-RWJ Medical School,undefined
[8] 675 Hoes Lane West,undefined
[9] Piscataway,undefined
[10] New Jersey 08854,undefined
[11] USA,undefined
[12] University of Washington School of Medicine,undefined
[13] 1959 NE Pacific Street,undefined
[14] Seattle,undefined
[15] Washington 98195,undefined
[16] USA,undefined
来源：
Nature | 2011年 / 479卷
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摘要：
The binding of helicase to viral RNA and the resulting activation of the retinoic acid inducible gene-I (RIG-I) are central to the innate immune response to viral infection. The structure of the RIG-I helicase domain with its repressor domain, in complex with double-stranded RNA, has now been determined. The structure suggests a mechanism of dsRNA translocation. Because RIG-I is homologous to many other helicases, such as Dicer of the RNAi machinery and the FANCM helicases involved in DNA repair, the structure should prove relevant to helicases in these other biological processes.
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页码：423 / 427
页数：4
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