Crystal structure of TB-RBP, a novel RNA-binding and regulating protein

J Mol Biol. 2002 Jun 21;319(5):1049-57. doi: 10.1016/S0022-2836(02)00364-9.


The testis/brain-RNA-binding protein (TB-RBP) spatially and temporally controls the expression of specific mRNAs in developing male germ cells and brain cells, and is implicated in DNA recombination and repair events. We report the 2.65 A crystal structure of mouse TB-RBP. The structure is predominantly alpha-helical and exhibits a novel protein fold and mode of assembly. Crystal symmetry and molecular symmetry combine to form an octet of TB-RBP monomers in the shape of an elongated spherical particle with a large cavity at its center. Amino acid residues that affect RNA and DNA binding are located on the interior surface of the assembled particle, and a putative nucleotide-binding domain that controls RNA binding is located at a dimer interface. Other modes of assembly are suggested for TB-RBP based on our structure and recently reported electron microscopic reconstructions of human TB-RBP.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • Dimerization
  • Guanosine Triphosphate / metabolism
  • Mice
  • Microscopy, Electron
  • Microtubule-Associated Proteins / chemistry*
  • Microtubule-Associated Proteins / metabolism*
  • Microtubule-Associated Proteins / ultrastructure
  • Models, Molecular
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • RNA / chemistry
  • RNA / metabolism*
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / metabolism*
  • RNA-Binding Proteins / ultrastructure


  • Microtubule-Associated Proteins
  • RNA-Binding Proteins
  • STRBP protein, human
  • RNA
  • Guanosine Triphosphate

Associated data

  • PDB/1KEY