6le1
Structure of RRM2 domain of DND1 protein
Structural highlights
Function[DND1_HUMAN] RNA-binding factor that positively regulates gene expression by prohibiting miRNA-mediated gene suppression. Relieves miRNA repression in germline cells (By similarity). Prohibits the function of several miRNAs by blocking the accessibility of target mRNAs. Sequence-specific RNA-binding factor that binds specifically to U-rich regions (URRs) in the 3' untranslated region (3'-UTR) of several mRNAs. Does not bind to miRNAs. May play a role during primordial germ cell (PGC) survival (By similarity). However, does not seem to be essential for PGC migration (By similarity).[1] Publication Abstract from PubMedRNA recognition motif (RRM) being the most abundant RNA binding domain in eukaryotes, is a major player in cellular regulation. Several variations in the canonical betaalphabetabetaalphabeta topology have been observed. We have determined the 2.3 A crystal structure of the human DND1-RRM2 domain. The structure revealed an interesting non-canonical RRM fold, which is maintained by the formation of a 3D domain swapped dimer between beta1 and beta4 strands across protomers. We have delineated the structural basis of the stable domain swapped dimer formation using the residue level dynamics of protein explored by NMR spectroscopy and MD simulations. Our structural and dynamics studies substantiate major determinants and molecular basis for domain swapped dimerization observed in the RRM domain. Human DND1-RRM2 forms a non-canonical domain swapped dimer.,Kumari P, Bhavesh NS Protein Sci. 2021 Apr 16. doi: 10.1002/pro.4083. PMID:33860980[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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