title: NMR resonance assignments of caspase recruitment domain of RIP2 kinase.
abstract: Receptor interacting protein-2, RIP2, is a serine/threonine kinase and has sequence homology to RIP. It functions as an adaptor molecule for some members from the tumor necrosis factor receptor family and mediates divergent signaling pathways including NF-κB activation and cell death. RIP2 contains an N-terminal kinases domain and a C-terminal caspase activation and recruitment domain (CARD). The apoptotic activity of RIP2 is restricted to its C-terminal CARD domain while NF-κB activation requires the intact RIP2 for binding. RIP2 CARD involved homotypic or heterotypic interactions with members of the death domains superfamily. Here I report backbone and sidechain (1)H, (13)C and (15)N resonance assignments of soluble RIP2 CARD as a basis for further structural and functional studies.
authors.affiliation: School of Life Sciences, Tianjin University, Tianjin, 300072, People's Republic of China. linzhi@linzhi.net.|Department of Physiology, National University of Singapore, Singapore, 117597, Singapore. linzhi@linzhi.net.|Life Sciences Institute, National University of Singapore, Singapore, 117456, Singapore. linzhi@linzhi.net.
authors.forename: Zhi
authors.identifier: 0000-0002-8902-4935
authors.initials: Z
authors.lastname: Lin
mesh_terms: D000595:Amino Acid Sequence; D020169:Caspases / Q000378:metabolism*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D000072417:Protein Domains; D053475:Receptor-Interacting Protein Serine-Threonine Kinase 2 / Q000737:chemistry* / Q000378:metabolism*
chemical_list: C506253:RIPK2 protein, human; D053475:Receptor-Interacting Protein Serine-Threonine Kinase 2; D020169:Caspases
keywords: Assignment; CARD; NMR; RIP2