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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography	IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties Robert Dagil , Neil J Ball , Roksana Ogrodowicz , Fruzsina Hobor , Andrew G. Purkiss , Geoff Kelly , Stephen R Martin , Ian A. Taylor , Andres Ramos Nucleic Acids Research 97 DOI: 10.1093/nar/gkz136 Diamond Proposal Number(s): [13775] Open Access Show Abstract ▼ 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. Importantly, the high-affinity RNA-binding by KH1KH2 is achieved by an inter-domain coupling 50-fold stronger than that existing in a second pseudo-dimer in the protein, KH3KH4. The presence of this strong coupling supports a role of RNA re-modelling in IMP1 recognition of known cancer targets.	Mar 2019

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I02-Macromolecular Crystallography

IMP1 KH1 and KH2 domains create a structural platform with unique RNA recognition and re-modelling properties

Robert Dagil , Neil J Ball , Roksana Ogrodowicz , Fruzsina Hobor , Andrew G. Purkiss , Geoff Kelly , Stephen R Martin , Ian A. Taylor , Andres Ramos

Nucleic Acids Research 97

DOI: 10.1093/nar/gkz136

Diamond Proposal Number(s): [13775]