1key

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

Structural highlights

1key is a 4 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[TSN_MOUSE] DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. Seems to recognize single-stranded DNA ends generated by staggered breaks occurring at recombination hot spots.^[1] Exhibits both single-stranded and double-stranded endoribonuclease activity. May act as an activator of RNA-induced silencing complex (RISC) by facilitating endonucleolytic cleavage of the siRNA passenger strand.^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wang J, Boja ES, Oubrahim H, Chock PB. Testis brain ribonucleic acid-binding protein/translin possesses both single-stranded and double-stranded ribonuclease activities. Biochemistry. 2004 Oct 26;43(42):13424-31. PMID:15491149 doi:http://dx.doi.org/10.1021/bi048847l
↑ Wang J, Boja ES, Oubrahim H, Chock PB. Testis brain ribonucleic acid-binding protein/translin possesses both single-stranded and double-stranded ribonuclease activities. Biochemistry. 2004 Oct 26;43(42):13424-31. PMID:15491149 doi:http://dx.doi.org/10.1021/bi048847l
↑ Pascal JM, Hart PJ, Hecht NB, Robertus JD. Crystal structure of TB-RBP, a novel RNA-binding and regulating protein. J Mol Biol. 2002 Jun 21;319(5):1049-57. PMID:12079346 doi:10.1016/S0022-2836(02)00364-9

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OCA

[1] Wang J, Boja ES, Oubrahim H, Chock PB. Testis brain ribonucleic acid-binding protein/translin possesses both single-stranded and double-stranded ribonuclease activities. Biochemistry. 2004 Oct 26;43(42):13424-31. PMID:15491149 doi:http://dx.doi.org/10.1021/bi048847l

[2] Wang J, Boja ES, Oubrahim H, Chock PB. Testis brain ribonucleic acid-binding protein/translin possesses both single-stranded and double-stranded ribonuclease activities. Biochemistry. 2004 Oct 26;43(42):13424-31. PMID:15491149 doi:http://dx.doi.org/10.1021/bi048847l

[3] Pascal JM, Hart PJ, Hecht NB, Robertus JD. Crystal structure of TB-RBP, a novel RNA-binding and regulating protein. J Mol Biol. 2002 Jun 21;319(5):1049-57. PMID:12079346 doi:10.1016/S0022-2836(02)00364-9

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