1key
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Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)
OverviewOverview
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.
About this StructureAbout this Structure
1KEY is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of TB-RBP, a novel RNA-binding and regulating protein., Pascal JM, Hart PJ, Hecht NB, Robertus JD, J Mol Biol. 2002 Jun 21;319(5):1049-57. PMID:12079346
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