1KEY

Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)

1KEY の概要

• エントリーDOI: 10.2210/pdb1key/pdb
• 分子名称: translin (2 entities in total)
• 機能のキーワード: rna-binding protein, tetramer/octamer assembly, apotb-rbp, rna binding protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm (By similarity): Q62348
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 107710.62

構造登録者

Pascal, J.M.,Hart, P.J.,Hecht, N.B.,Robertus, J.D. (登録日: 2001-11-19, 公開日: 2002-07-03, 最終更新日: 2024-02-07)

主引用文献

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

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: 12079346
DOI: 10.1016/S0022-2836(02)00364-9

実験手法

X-RAY DIFFRACTION (2.65 Å)