1KEY
Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)
Summary for 1KEY
| Entry DOI | 10.2210/pdb1key/pdb |
| Descriptor | translin (2 entities in total) |
| Functional Keywords | rna-binding protein, tetramer/octamer assembly, apotb-rbp, rna binding protein |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm (By similarity): Q62348 |
| Total number of polymer chains | 4 |
| Total formula weight | 107710.62 |
| Authors | Pascal, J.M.,Hart, P.J.,Hecht, N.B.,Robertus, J.D. (deposition date: 2001-11-19, release date: 2002-07-03, Last modification date: 2024-02-07) |
| Primary citation | Pascal, J.M.,Hart, P.J.,Hecht, N.B.,Robertus, J.D. Crystal Structure of TB-RBP, a Novel RNA-binding and Regulating Protein J.Mol.Biol., 319:1049-1057, 2002 Cited by 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. PubMed: 12079346DOI: 10.1016/S0022-2836(02)00364-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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