title: Structural domains in RNAi.
abstract: Structural and biochemical studies have begun to elucidate the pathway of RNA silencing that leads to the formation of the RISC complex. The outstanding feature of this pathway is the precise recognition and processing of double-stranded RNA. We present a review of recent structures that illustrate the molecular mechanisms contributing to these two related functions, highlighting models of Drosha, Dicer, and RISC function.
authors.affiliation: Department of Biochemistry, Emory University, 1510 Clifton Road, Atlanta, GA 30322, USA.
authors.forename: Robert E
authors.initials: RE
authors.lastname: Collins
authors.forename: Xiaodong
authors.initials: X
authors.lastname: Cheng
mesh_terms: D000818:Animals; D001665:Binding Sites; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D020868:Gene Silencing; D005821:Genetic Techniques; D006801:Humans; D035683:MicroRNAs / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D019711:Pyrococcus / Q000378:metabolism; D012313:RNA / Q000737:chemistry*; D034622:RNA Interference; D012330:RNA, Double-Stranded / Q000737:chemistry; D034743:RNA-Induced Silencing Complex / Q000502:physiology; D016914:Ribonuclease H / Q000737:chemistry; D043244:Ribonuclease III / Q000737:chemistry* / Q000502:physiology
chemical_list: D035683:MicroRNAs; D012330:RNA, Double-Stranded; D034743:RNA-Induced Silencing Complex; D012313:RNA; C517918:DROSHA protein, human; D043244:Ribonuclease III; D016914:Ribonuclease H