Novel RNA recognition motif domain in the cytoplasmic polyadenylation element binding protein 3

Proteins. 2014 Oct;82(10):2879-86. doi: 10.1002/prot.24651. Epub 2014 Aug 11.

Abstract

The family of cytoplasmic polyadenylation element binding proteins CPEB1, CPEB2, CPEB3, and CPEB4 binds to the 3'-untranslated region (3'-UTR) of mRNA, and plays significant roles in mRNA metabolism and translation regulation. They have a common domain organization, involving two consecutive RNA recognition motif (RRM) domains followed by a zinc finger domain in the C-terminal region. We solved the solution structure of the first RRM domain (RRM1) of human CPEB3, which revealed that CPEB3 RRM1 exhibits structural features distinct from those of the canonical RRM domain. Our structural data provide important information about the RNA binding ability of CPEB3 RRM1.

Keywords: 3′-UTR; CPE; CPEB3; GluR2; Mrna; NMR; RRM; structure.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3' Untranslated Regions
  • Amino Acid Sequence
  • Binding Sites
  • Conserved Sequence
  • Databases, Protein
  • Humans
  • Models, Molecular*
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Fragments / chemistry*
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Protein Interaction Domains and Motifs
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Protein Stability
  • Protein Structure, Secondary
  • RNA, Messenger / metabolism
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Sequence Alignment
  • Solubility

Substances

  • 3' Untranslated Regions
  • CPEB3 protein, human
  • Peptide Fragments
  • Protein Isoforms
  • RNA, Messenger
  • RNA-Binding Proteins
  • Recombinant Proteins

Associated data

  • PDB/2RUG