This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1key
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1key.gif|left|200px]] | [[Image:1key.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1key", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | | | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | + | --> | |
| - | + | {{STRUCTURE_1key| PDB=1key | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)''' | '''Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)''' | ||
| Line 29: | Line 26: | ||
[[Category: Pascal, J M.]] | [[Category: Pascal, J M.]] | ||
[[Category: Robertus, J D.]] | [[Category: Robertus, J D.]] | ||
| - | [[Category: | + | [[Category: Apotb-rbp]] |
| - | [[Category: | + | [[Category: Rna-binding protein]] |
| - | [[Category: | + | [[Category: Tetramer/octamer assembly]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:39:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:39, 2 May 2008
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 Fri May 2 22:39:41 2008
