6BZH

Structure of mouse RIG-I tandem CARDs

Summary for 6BZH

• Entry DOI: 10.2210/pdb6bzh/pdb
• Descriptor: Probable ATP-dependent RNA helicase DDX58, 1,2-ETHANEDIOL, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: card rig-i dead-box rna helicases, hydrolase
• Biological source: Mus musculus (Mouse)
• Cellular location: Cytoplasm : Q6Q899
• Total number of polymer chains: 5
• Total formula weight: 113948.36

Authors

Kershaw, N.J.,D'Cruz, A.A.,Babon, J.J.,Nicholson, S.E. (deposition date: 2017-12-24, release date: 2018-01-17, Last modification date: 2023-10-04)

Primary citation

D'Cruz, A.A.,Kershaw, N.J.,Hayman, T.J.,Linossi, E.M.,Chiang, J.J.,Wang, M.K.,Dagley, L.F.,Kolesnik, T.B.,Zhang, J.G.,Masters, S.L.,Griffin, M.D.W.,Gack, M.U.,Murphy, J.M.,Nicola, N.A.,Babon, J.J.,Nicholson, S.E.
Identification of a second binding site on the TRIM25 B30.2 domain.
Biochem. J., 475:429-440, 2018

PubMed Abstract: The etinoic acid-nducible ene- (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 partite otif 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 (aspase ctivation and ecruitment omains) 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.

PubMed: 29259080
DOI: 10.1042/BCJ20170427

Experimental method

X-RAY DIFFRACTION (2.5 Å)