page_title: RNA recognition motif
hierarchical_section_title: RNA recognition motif
caption_attribution_description: English: Structure of an RNA recognition motif (RRM), showing the fold with the typical with beta-alpha-beta-beta-alpha-beta architecture. Generated with Pymol from PDB entry 2CQI
context_page_description: RNA recognition motif, RNP-1 is a putative RNA-binding domain of about 90 amino acids that are known to bind single-stranded RNAs. It was found in many eukaryotic proteins.
  The largest group of single strand RNA-binding protein is the eukaryotic RNA recognition motif family that contains an eight amino acid RNP-1 consensus sequence.
  RRM proteins have a variety of RNA binding preferences and functions, and include heterogeneous nuclear ribonucleoproteins, proteins implicated in regulation of alternative splicing, protein components of small nuclear ribonucleoproteins, and proteins that regulate RNA stability and translation. The RRM in heterodimeric splicing factor U2 snRNP auxiliary factor appears to have two RRM-like domains with specialised features for protein recognition. The motif also appears in a few single stranded DNA binding proteins.
  The typical RRM consists of four anti-parallel beta-strands and two alpha-helices arranged in a beta-alpha-beta-beta-alpha-beta fold with side chains that stack with RNA bases. A third helix is present during RNA binding in some cases. The RRM is reviewed in a number of publications.
context_section_description: RNA recognition motif, RNP-1 is a putative RNA-binding domain of about 90 amino acids that are known to bind single-stranded RNAs. It was found in many eukaryotic proteins.
  The largest group of single strand RNA-binding protein is the eukaryotic RNA recognition motif (RRM) family that contains an eight amino acid RNP-1 consensus sequence.
  RRM proteins have a variety of RNA binding preferences and functions, and include heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing (SR, U2AF2, Sxl), protein components of small nuclear ribonucleoproteins (U1 and U2 snRNPs), and proteins that regulate RNA stability and translation (PABP, La, Hu). The RRM in heterodimeric splicing factor U2 snRNP auxiliary factor appears to have two RRM-like domains with specialised features for protein recognition. The motif also appears in a few single stranded DNA binding proteins.
  The typical RRM consists of four anti-parallel beta-strands and two alpha-helices arranged in a beta-alpha-beta-beta-alpha-beta fold with side chains that stack with RNA bases.  A third helix is present during RNA binding in some cases. The RRM is reviewed in a number of publications.
caption: Typical architecture of an RRM domain, with a four-stranded antiparallel beta-sheet, stacked on two alpha helices
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