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1key

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Revision as of 21:21, 24 January 2018

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, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1key"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Mouse Testis/Brain RNA-binding Protein (TB-RBP)==
 <StructureSection load='1key' size='340' side='right' caption='[[1key]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1key]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KEY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KEY FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1key FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1key OCA], [http://pdbe.org/1key PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1key RCSB], [http://www.ebi.ac.uk/pdbsum/1key PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1key FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1key OCA], [http://pdbe.org/1key PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1key RCSB], [http://www.ebi.ac.uk/pdbsum/1key PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1key ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ke/1key_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ke/1key_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1key

From Proteopedia

Revision as of 21:21, 24 January 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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