+1 Recommend
0 collections
      • Record: found
      • Abstract: found
      • Article: not found

      Structure of PTB bound to RNA: specific binding and implications for splicing regulation.

      Science (New York, N.Y.)
      Alternative Splicing, Amino Acid Sequence, Base Sequence, Binding Sites, Exons, Heterogeneous-Nuclear Ribonucleoproteins, chemistry, genetics, metabolism, Humans, Hydrogen Bonding, Hydrophobic and Hydrophilic Interactions, Models, Molecular, Molecular Sequence Data, Mutation, Nuclear Magnetic Resonance, Biomolecular, Nuclear Proteins, Oligoribonucleotides, Polypyrimidine Tract-Binding Protein, Protein Binding, Protein Conformation, Protein Structure, Tertiary, RNA, Ribonucleoproteins

      Read this article at

          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.


          The polypyrimidine tract binding protein (PTB) is a 58-kilodalton RNA binding protein involved in multiple aspects of messenger RNA metabolism, including the repression of alternative exons. We have determined the solution structures of the four RNA binding domains (RBDs) of PTB, each bound to a CUCUCU oligonucleotide. Each RBD binds RNA with a different binding specificity. RBD3 and RBD4 interact, resulting in an antiparallel orientation of their bound RNAs. Thus, PTB will induce RNA looping when bound to two separated pyrimidine tracts within the same RNA. This leads to structural models for how PTB functions as an alternative-splicing repressor.

          Related collections

          Author and article information


          Comment on this article