{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dagil R"],"funding":["Cancer Research UK","Wellcome trust","Medical Research Council","The Francis Crick Institute","Wellcome Trust"],"pagination":["4334-4348"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6486635"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["47(8)"],"pubmed_abstract":["IGF2 mRNA-binding protein 1 (IMP1) is a key regulator of messenger RNA (mRNA) metabolism and transport in organismal development and, in cancer, its mis-regulation is an important component of tumour metastasis. IMP1 function relies on the recognition of a diverse set of mRNA targets that is mediated by the combinatorial action of multiple RNA-binding domains. Here, we dissect the structure and RNA-binding properties of two key RNA-binding domains of IMP1, KH1 and KH2, and we build a kinetic model for the recognition of RNA targets. Our data and model explain how the two domains are organized as an intermolecular pseudo-dimer and that the important role they play in mRNA target recognition is underpinned by the high RNA-binding affinity and fast kinetics of this KH1KH2-RNA recognition unit"],"journal":["Nucleic acids research"],"pubmed_title":["IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties."],"pmcid":["PMC6486635"],"funding_grant_id":["10029","MC_U117574558","FC001029","U117574558","FC001178","MC_PC_13051","10178","10015"],"pubmed_authors":["Taylor IA","Dagil R","Hobor F","Kelly G","Ball NJ","Purkiss AG","Ramos A","Martin SR","Ogrodowicz RW"],"additional_accession":[]},"is_claimable":false,"name":"IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties.","description":"IGF2 mRNA-binding protein 1 (IMP1) is a key regulator of messenger RNA (mRNA) metabolism and transport in organismal development and, in cancer, its mis-regulation is an important component of tumour metastasis. IMP1 function relies on the recognition of a diverse set of mRNA targets that is mediated by the combinatorial action of multiple RNA-binding domains. Here, we dissect the structure and RNA-binding properties of two key RNA-binding domains of IMP1, KH1 and KH2, and we build a kinetic model for the recognition of RNA targets. Our data and model explain how the two domains are organized as an intermolecular pseudo-dimer and that the important role they play in mRNA target recognition is underpinned by the high RNA-binding affinity and fast kinetics of this KH1KH2-RNA recognition unit","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 May","modification":"2026-04-30T02:36:59.327Z","creation":"2019-06-06T22:50:10Z"},"accession":"S-EPMC6486635","cross_references":{"pubmed":["30864660"],"doi":["10.1093/nar/gkz136"]}}