1KEY

Crystal Structure of TB-RBP, a Novel RNA-binding and Regulating Protein

(2002) J Mol Biol 319: 1049-1057

• PubMed: 12079346 Search on PubMed
• DOI: https://doi.org/10.1016/S0022-2836(02)00364-9
• Primary Citation of Related Structures:  
  1KEY


• PubMed Abstract: 
  

  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.

   View More

---

Organizational Affiliation: 

Institute for Cellular and Molecular Biology and the Department of Chemistry and Biochemistry, University of Texas at Austin, 78712, USA.