Journal article
Crystal structure of the TRIM25 B30.2 (PRYSPRY) domain: A key component of antiviral signalling
AA D'Cruz, NJ Kershaw, JJ Chiang, MK Wang, NA Nicola, JJ Babon, MU Gack, SE Nicholson
Biochemical Journal | PORTLAND PRESS LTD | Published : 2013
DOI: 10.1042/BJ20121425
Abstract
TRIM (tripartite motif) proteins primarily function as ubiquitin E3 ligases that regulate the innate immune response to infection. TRIM25 [also known as Efp (oestrogen-responsive finger protein)] has been implicated in the regulation of oestrogen receptor α signalling and in the regulation of innate immune signalling via RIG-I (retinoic acid-inducible gene-I). RIG-I senses cytosolic viralRNAand is subsequently ubiquitinated by TRIM25 at its N-terminal CARDs (caspase recruitment domains), leading to type I interferon production. The interaction with RIG-I is dependent on the TRIM25 B30.2 domain, a protein-interaction domain composed of the PRYand SPRYtandem sequencemotifs. In the present stud..
View full abstractGrants
Awarded by National Institute of Allergy and Infectious Diseases
Funding Acknowledgements
This work was supported, in part, by the National Health and Medical Research Council (NHMRC) Australia [grant numbers 461219, 637348, 487922 and 3616461 and fellowships to S.E.N. and N.A.N., the Victorian State Government Operational Infrastructure Scheme grant, the U.S. National Institutes of Health [grant number R01 AI087846 (to MUG.)], the Australian Postgraduate Awards (to A.A.D.) and the Australian Research Council via a Future Fellowship to J.J.B.