title: Crystallization of mouse RIG-I ATPase domain: in situ proteolysis.
abstract: RIG-I is a key pattern recognition receptor that recognizes cytoplasmic viral RNA. Upon ligand binding, it undergoes a conformational change that induces an active signaling conformation. However, the details of this conformational change remain elusive until high-resolution crystal structures of different functional conformations are available. X-ray crystallography is a powerful tool to study structure-function relationships, but crystallization is often the limiting step of the method. Here, we describe the in situ in-drop proteolysis of RIG-I that yielded crystals of the ATPase domain of mouse RIG-I suitable for structure determination.
authors: Department of Biochemistry at the Gene Center, Ludwig-Maximilians-University Munich, Feodor-Lynen-Strasse 25, 81377, Munich, Germany.
authors: Filiz
authors: F
authors: Civril
authors: Karl-Peter
authors: KP
authors: Hopfner
mesh_terms: D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D053487:DEAD-box RNA Helicases / Q000737:chemistry* / Q000378:metabolism; D007113:Immunity, Innate; D051379:Mice; D011487:Protein Conformation; D059748:Proteolysis; D012367:RNA, Viral / Q000737:chemistry
chemical_list: D012367:RNA, Viral; D053487:DEAD-box RNA Helicases