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

(Difference between revisions)

Jump to: navigation, search

Revision as of 06:52, 11 August 2021

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 3: / Line 3: @@
 <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>
+<table><tr><td colspan='2'>[[1key]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1key ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1key FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1key OCA], [https://pdbe.org/1key PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1key RCSB], [https://www.ebi.ac.uk/pdbsum/1key PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1key ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TSN_MOUSE 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.<ref>PMID:15491149</ref>   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.<ref>PMID:15491149</ref>
+[[https://www.uniprot.org/uniprot/TSN_MOUSE 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.<ref>PMID:15491149</ref>   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.<ref>PMID:15491149</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1key

From Proteopedia

Revision as of 06:52, 11 August 2021

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

Personal tools

Navigation

Search

Toolbox