page_title: RNA-binding protein
section_title: Double-stranded RNA-binding motif
hierarchical_section_title: RNA-binding protein / Protein–RNA interactions / Double-stranded RNA-binding motif
caption_attribution_description: English: Cartoon representation of the molecular structure of protein registered with 2b7t code. Deutsch: Grafik des Molekularstruktur von jenem Protein, das mit 2b7t code registriert ist. Plattdüütsch: Grafik, de de Molekularstruktur von dat Protein wiest, dat mit’n Kood 2b7t registreert is.
context_page_description: RNA-binding proteins are proteins that bind to the double or single stranded RNA in cells and participate in forming ribonucleoprotein complexes.
  RBPs contain various structural motifs, such as RNA recognition motif, dsRNA binding domain, zinc finger and others.
  They are cytoplasmic and nuclear proteins. However, since most mature RNA is exported from the nucleus relatively quickly, most RBPs in the nucleus exist as complexes of protein and pre-mRNA called heterogeneous ribonucleoprotein particles.
  RBPs have crucial roles in various cellular processes such as: cellular function, transport and localization. They especially play a major role in post-transcriptional control of RNAs, such as: splicing, polyadenylation, mRNA stabilization, mRNA localization and translation. Eukaryotic cells encode diverse RBPs, approximately 500 genes, with unique RNA-binding activity and protein–protein interaction. During evolution, the diversity of RBPs greatly increased with the increase in the number of introns. Diversity enabled eukaryotic cells to utilize RNA exons in various arrangements, giving rise to a unique RNP for each RNA.
context_section_description: The double-stranded RNA-binding motif (dsRM, dsRBD), a 70–75 amino-acid domain, plays a critical role in RNA processing, RNA localization, RNA interference, RNA editing, and translational repression. All three structures of the domain solved as of 2005 possess uniting features that explain how dsRMs only bind to dsRNA instead of dsDNA. The dsRMs were found to interact along the RNA duplex via both α-helices and β1-β2 loop. Moreover, all three dsRBM structures make contact with the sugar-phosphate backbone of the major groove and of one minor groove, which is mediated by the β1-β2 loop along with the N-terminus region of the alpha helix 2. This interaction is a unique adaptation for the shape of an RNA double helix as it involves 2'-hydroxyls and phosphate oxygen. Despite the common structural features among dsRBMs, they exhibit distinct chemical frameworks, which permits specificity for a variety for RNA structures including stem-loops, internal loops, bulges or helices containing mismatches.
caption: dsRBD from rat ADAR2 protein (PDB: 2b7t​).
exif: {}