6fq1 | pdb_00006fq1
Crystal structure of the RRM12 domain of IMP3
Structural highlights
Function[IF2B3_HUMAN] RNA-binding factor that may recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to beta-actin/ACTB and MYC transcripts. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs.[1] [2] Publication Abstract from PubMedThe IMP family of RNA binding proteins, also named as insulin-like growth factor 2 (IGF2) mRNA-binding proteins (IGF2BPs), are highly conserved RNA regulators that are involved in many RNA processing stages, including mRNA stability, localization and translation. There are three paralogs in the IMP family, IMP1-3, in mammals that all adopt the same domain arrangement with two RNA recognition motifs (RRM) in the N-terminus and four KH domains in the C-terminus. Here, we report the structure and biochemical characterization of IMP3 RRM12 and its complex with two short RNAs. These structures show that both RRM domains of IMP3 adopt the canonical RRM topology with two alpha-helices packed on an anti-parallel four stranded beta-sheet. The spatial orientation of RRM1 to RRM2 is unique compared with other known tandem RRM structures. In the IMP3 RRM12 complex with RNA, only RRM1 is involved in RNA binding and recognizes a dinucleotide sequence. Structural basis of IMP3 RRM12 recognition of RNA.,Jia M, Gut H, Chao JA RNA. 2018 Aug 22. pii: rna.065649.118. doi: 10.1261/rna.065649.118. PMID:30135093[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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