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3h8z

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Revision as of 07:25, 1 November 2017

The Crystal Structure of the Tudor Domains from FXR2

Structural highlights

3h8z is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	FXR2, FMR1L2 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FXR2_HUMAN] RNA-binding protein.

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

BACKGROUND: Expansion of the CGG trinucleotide repeat in the 5'-untranslated region of the FMR1, fragile X mental retardation 1, gene results in suppression of protein expression for this gene and is the underlying cause of Fragile X syndrome. In unaffected individuals, the FMRP protein, together with two additional paralogues (Fragile X Mental Retardation Syndrome-related Protein 1 and 2), associates with mRNA to form a ribonucleoprotein complex in the nucleus that is transported to dendrites and spines of neuronal cells. It is thought that the fragile X family of proteins contributes to the regulation of protein synthesis at sites where mRNAs are locally translated in response to stimuli. METHODOLOGY/PRINCIPAL FINDINGS: Here, we report the X-ray crystal structures of the non-canonical nuclear localization signals of the FXR1 and FXR2 autosomal paralogues of FMRP, which were determined at 2.50 and 1.92 A, respectively. The nuclear localization signals of the FXR1 and FXR2 comprise tandem Tudor domain architectures, closely resembling that of UHRF1, which is proposed to bind methylated histone H3K9. CONCLUSIONS: The FMRP, FXR1 and FXR2 proteins comprise a small family of highly conserved proteins that appear to be important in translational regulation, particularly in neuronal cells. The crystal structures of the N-terminal tandem Tudor domains of FXR1 and FXR2 revealed a conserved architecture with that of FMRP. Biochemical analysis of the tandem Tudor domains reveals their ability to preferentially recognize trimethylated peptides in a sequence-specific manner. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.

Structural studies of the tandem Tudor domains of fragile X mental retardation related proteins FXR1 and FXR2.,Adams-Cioaba MA, Guo Y, Bian C, Amaya MF, Lam R, Wasney GA, Vedadi M, Xu C, Min J PLoS One. 2010 Nov 2;5(11):e13559. PMID:21072162^[1]

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

References

↑ Adams-Cioaba MA, Guo Y, Bian C, Amaya MF, Lam R, Wasney GA, Vedadi M, Xu C, Min J. Structural studies of the tandem Tudor domains of fragile X mental retardation related proteins FXR1 and FXR2. PLoS One. 2010 Nov 2;5(11):e13559. PMID:21072162 doi:10.1371/journal.pone.0013559

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/3h8z"

@@ Line 1: / Line 1: @@
 ==The Crystal Structure of the Tudor Domains from FXR2==
 <StructureSection load='3h8z' size='340' side='right' caption='[[3h8z]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FXR2, FMR1L2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3h8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8z OCA], [http://pdbe.org/3h8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h8z RCSB], [http://www.ebi.ac.uk/pdbsum/3h8z PDBsum]</span></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=3h8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h8z OCA], [http://pdbe.org/3h8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h8z RCSB], [http://www.ebi.ac.uk/pdbsum/3h8z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h8z ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 37: / Line 38: @@
 [[Category: Arrowsmith, C H]]
 [[Category: Bochkarev, A]]
-[[Category: Dong,A]]
+[[Category: Dong, A]]
 [[Category: Edwards, A M]]
 [[Category: Guo, Y]]

3h8z

From Proteopedia

Revision as of 07:25, 1 November 2017

The Crystal Structure of the Tudor Domains from FXR2

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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