Ontology highlight
ABSTRACT:
SUBMITTER: Scheiba RM
PROVIDER: S-EPMC4615805 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Scheiba Rafael M RM de Opakua Alain Ibáñez AI Díaz-Quintana Antonio A Cruz-Gallardo Isabel I Martínez-Cruz Luis A LA Martínez-Chantar María L ML Blanco Francisco J FJ Díaz-Moreno Irene I
RNA biology 20140101 10
Human antigen R (HuR) is a 32 kDa protein with 3 RNA Recognition Motifs (RRMs), which bind to Adenylate and uridylate Rich Elements (AREs) of mRNAs. Whereas the N-terminal and central domains (RRM1 and RRM2) are essential for AREs recognition, little is known on the C-terminal RRM3 beyond its implication in HuR oligomerization and apoptotic signaling. We have developed a detergent-based strategy to produce soluble RRM3 for structural studies. We have found that it adopts the typical RRM fold, do ...[more]