期刊
NUCLEIC ACIDS RESEARCH
卷 38, 期 15, 页码 5193-5205出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkq216
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资金
- Wellcome Trust [WT082088MA]
- MRC [U117574558]
- European Molecular Biology Organization (EMBO) [240-2005]
- Italian ISS [526D/39]
- ISS [527B/2B/6]
- Associazione Italiana per la Ricerca sul Cancro (AIRC)
- CIPE
- Medical Research Council [MC_U117574558, MC_U117533887] Funding Source: researchfish
- MRC [MC_U117533887, MC_U117574558] Funding Source: UKRI
KSRP is a multi-domain RNA-binding protein that recruits the exosome-containing mRNA degradation complex to mRNAs coding for cellular proliferation and inflammatory response factors. The selectivity of this mRNA degradation mechanism relies on KSRP recognition of AU-rich elements in the mRNA 3'UTR, that is mediated by KSRP's KH domains. Our structural analysis shows that the inter-domain linker orients the two central KH domains of KSRP-and their RNA-binding surfaces-creating a two-domain unit. We also show that this inter-domain arrangement is important to the interaction with KSRP's RNA targets.
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