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Identification of a second binding site on the TRIM25 B30.2 domain
- Source :
- Biochemical Journal. 475:429-440
- Publication Year :
- 2018
- Publisher :
- Portland Press Ltd., 2018.
-
Abstract
- The retinoic acid-inducible gene-I (RIG-I) receptor recognizes short 5′-di- and triphosphate base-paired viral RNA and is a critical mediator of the innate immune response against viruses such as influenza A, Ebola, HIV and hepatitis C. This response is reported to require an orchestrated interaction with the tripartite motif 25 (TRIM25) B30.2 protein-interaction domain. Here, we present a novel second RIG-I-binding interface on the TRIM25 B30.2 domain that interacts with CARD1 and CARD2 (caspase activation and recruitment domains) of RIG-I and is revealed by the removal of an N-terminal α-helix that mimics dimerization of the full-length protein. Further characterization of the TRIM25 coiled-coil and B30.2 regions indicated that the B30.2 domains move freely on a flexible tether, facilitating RIG-I CARD recruitment. The identification of a dual binding mode for the TRIM25 B30.2 domain is a first for the SPRY/B30.2 domain family and may be a feature of other SPRY/B30.2 family members.
- Subjects :
- Models, Molecular
Protein Conformation, alpha-Helical
0301 basic medicine
TRIM25
Recombinant Fusion Proteins
viruses
Genetic Vectors
Receptors, Cytoplasmic and Nuclear
Plasma protein binding
B30.2-SPRY Domain
Crystallography, X-Ray
Biochemistry
Article
Mice
03 medical and health sciences
Protein structure
Escherichia coli
Animals
Humans
Histidine
Protein Interaction Domains and Motifs
Amino Acid Sequence
Cloning, Molecular
Receptors, Immunologic
Binding site
DEAD Box Protein 58
Molecular Biology
Glutathione Transferase
Sequence Deletion
Binding Sites
biology
RIG-I
Chemistry
virus diseases
Signal transducing adaptor protein
Cell Biology
Recombinant Proteins
Cell biology
Ubiquitin ligase
HEK293 Cells
030104 developmental biology
Caspase Activation and Recruitment Domain
biology.protein
Protein Conformation, beta-Strand
Oligopeptides
Protein Binding
Subjects
Details
- ISSN :
- 14708728 and 02646021
- Volume :
- 475
- Database :
- OpenAIRE
- Journal :
- Biochemical Journal
- Accession number :
- edsair.doi.dedup.....798397e94e702c0bf6ce404947881d06