2x04

From Proteopedia

(Difference between revisions)

Revision as of 09:12, 3 October 2018

Crystal structure of the PABC-TNRC6C complex

Structural highlights

2x04 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1jgn, 1jh4, 1g9l, 2dkl, 1cvj
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PABP1_HUMAN] Binds the poly(A) tail of mRNA. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed.^[1] ^[2] [TNR6C_HUMAN] Plays a role in RNA-mediated gene silencing by micro-RNAs (miRNAs). Required for miRNA-dependent translational repression of complementary mRNAs by argonaute family proteins.^[3]

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

GW182-family proteins are essential for microRNA-mediated translational repression and deadenylation in animal cells. Here we show that a conserved motif in the human GW182 paralog TNRC6C interacts with the C-terminal domain of polyadenylate binding protein 1 (PABC) and present the crystal structure of the complex. Mutations at the complex interface impair mRNA deadenylation in mammalian cell extracts, suggesting that the GW182-PABC interaction contributes to microRNA-mediated gene silencing.

Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation.,Jinek M, Fabian MR, Coyle SM, Sonenberg N, Doudna JA Nat Struct Mol Biol. 2010 Feb;17(2):238-40. Epub 2010 Jan 24. PMID:20098421^[4]

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

References

↑ Grosset C, Chen CY, Xu N, Sonenberg N, Jacquemin-Sablon H, Shyu AB. A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. Cell. 2000 Sep 29;103(1):29-40. PMID:11051545
↑ Singh G, Rebbapragada I, Lykke-Andersen J. A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay. PLoS Biol. 2008 Apr 29;6(4):e111. doi: 10.1371/journal.pbio.0060111. PMID:18447585 doi:10.1371/journal.pbio.0060111
↑ Zipprich JT, Bhattacharyya S, Mathys H, Filipowicz W. Importance of the C-terminal domain of the human GW182 protein TNRC6C for translational repression. RNA. 2009 May;15(5):781-93. Epub 2009 Mar 20. PMID:19304925 doi:rna.1448009
↑ Jinek M, Fabian MR, Coyle SM, Sonenberg N, Doudna JA. Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation. Nat Struct Mol Biol. 2010 Feb;17(2):238-40. Epub 2010 Jan 24. PMID:20098421 doi:10.1038/nsmb.1768

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/2x04"

@@ Line 1: / Line 1: @@
-==CRYSTAL STRUCTURE OF THE PABC-TNRC6C COMPLEX==
+==Crystal structure of the PABC-TNRC6C complex==
 <StructureSection load='2x04' size='340' side='right' caption='[[2x04]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jgn|1jgn]], [[1jh4|1jh4]], [[1g9l|1g9l]], [[2dkl|2dkl]], [[1cvj|1cvj]]</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=2x04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x04 OCA], [http://pdbe.org/2x04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x04 RCSB], [http://www.ebi.ac.uk/pdbsum/2x04 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=2x04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x04 OCA], [http://pdbe.org/2x04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x04 RCSB], [http://www.ebi.ac.uk/pdbsum/2x04 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x04 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x0/2x04_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x0/2x04_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 38: / Line 39: @@
 [[Category: Jinek, M]]
 [[Category: Sonenberg, N]]
+[[Category: Coiled coil]]
 [[Category: Deadenylation]]
 [[Category: Methylation]]

2x04

From Proteopedia

Revision as of 09:12, 3 October 2018

Crystal structure of the PABC-TNRC6C complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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