Structural basis of RIP2 activation and signaling

• Main Authors: Gong, Q, Long, Z, Zhong, F.L, Teo, D.E.T, Jin, Y, Yin, Z, Boo, Z.Z, Zhang, Y, Zhang, J, Yang, R, Bhushan, S, Reversade, B, Li, Z, Wu, B
• Other Authors: PAEDIATRICS
• Format: Article
• Published: Nature Publishing Group 2020
• Subjects: adaptor protein; beta actin; caspase recruitment domain protein 15; caspase recruitment domain protein 4; caspase recruitment domain signaling protein; mitochondria antiviral signaling protein; monomer; nlrc4 protein; oligomer; receptor interacting protein serine threonine kinase 2; snap protein; unclassified drug; protein binding; recombinant protein; RIPK2 protein, human; bacterial disease; chemical binding; infectivity; molecular analysis; pathogen; protein; ultrastructure; Article; caspase activation and recruitment domain; cell organelle; controlled study; electron tomography; enzyme activation; enzyme activity; human; in vitro study; oligomerization; protein protein interaction; riposome; signal transduction; site directed mutagenesis; amino acid sequence; chemistry; cryoelectron microscopy; HEK293 cell line; metabolism; molecular model; protein domain; protein multimerization; structure activity relation; Bacteria (microorganisms); Mammalia; Amino Acid Sequence; CARD Signaling Adaptor Proteins; Cryoelectron Microscopy; HEK293 Cells; Humans; Models, Molecular; Protein Binding; Protein Domains; Protein Multimerization; Receptor-Interacting Protein Serine-Threonine Kinase 2; Recombinant Proteins; Signal Transduction; Structure-Activity Relationship
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/178379
• Institution: National University of Singapore

10.1038/s41467-018-07447-9