1key
From Proteopedia
(New page: 200px<br /><applet load="1key" size="450" color="white" frame="true" align="right" spinBox="true" caption="1key, resolution 2.65Å" /> '''Crystal Structure of...) |
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| - | [[Image:1key.gif|left|200px]]<br /><applet load="1key" size=" | + | [[Image:1key.gif|left|200px]]<br /><applet load="1key" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1key, resolution 2.65Å" /> | caption="1key, resolution 2.65Å" /> | ||
'''Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)'''<br /> | '''Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The testis/brain-RNA-binding protein (TB-RBP) spatially and temporally | + | 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 Structure== | ==About this Structure== | ||
| - | 1KEY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1KEY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hart, P | + | [[Category: Hart, P J.]] |
| - | [[Category: Hecht, N | + | [[Category: Hecht, N B.]] |
| - | [[Category: Pascal, J | + | [[Category: Pascal, J M.]] |
| - | [[Category: Robertus, J | + | [[Category: Robertus, J D.]] |
[[Category: apotb-rbp]] | [[Category: apotb-rbp]] | ||
[[Category: rna-binding protein]] | [[Category: rna-binding protein]] | ||
[[Category: tetramer/octamer assembly]] | [[Category: tetramer/octamer assembly]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:33:23 2008'' |
Revision as of 11:33, 21 February 2008
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Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)
Overview
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 Structure
1KEY is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:33:23 2008
