Evidence map›Paper›PMID 18824697›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Structural basis for RNA recognition by a type II poly(A)-binding protein.

Jikui Song, Jered V McGivern, Karl W Nichols, John L Markley, Michael D Sheets

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.4field-weighted citation impact, top 35% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. mRNA Interactome Capture from Plant Protoplasts.Journal of visualized experiments : JoVE · 2017
    Article
  5. Article
  6. Article
  7. Conformational stability of the RNP domain controls fibril formation of PABPN1.Protein science : a publication of the Protein Society · 2015
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Jikui SongDepartment of Biochemistry, Center for Eukaryotic Structural Genomics, University of Wisconsin, Madison, WI 53706, USA.
Jered V McGivern
Karl W Nichols
John L Markley
Michael D Sheets
University of Wisconsin–Madison · US

Funding

Specialized Center for Eukaryotic Structural GenomicsU54GM074901 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 2005 to 2009
$18.9M
WATER DISTRIB:PHYSICAL PROPERT:PIZZA &LMPS MOZZARELLA CHEESES:EARLY STAGE MATURP41RR002301 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI KEUTSCH, FRANK · 1985 to 2011
$13.0M
900 MHz NMR Spectrometer Biomolecular InvestigationsP41GM066326 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN L · 2002 to 2006
$5.0M
Control of Spemann's organizerR01HD043996 · NICHD · UNIVERSITY OF WISCONSIN-MADISON · PI SHEETS, MICHAEL D · 2003 to 2007
$1.3M
A novel embryonic poly(A) binding proteinR03HD044049 · NICHD · UNIVERSITY OF WISCONSIN MADISON · PI SHEETS, MICHAEL D · 2003 to 2004
$141k
NCRR NIH HHS P41 RR002301NCRR NIH HHS P41 RR02301NICHD NIH HHS R01 HD043996NICHD NIH HHS R01-HD43996NICHD NIH HHS R03 HD044049NICHD NIH HHS R03-HD-44049NIGMS NIH HHS P41 GM066326NIGMS NIH HHS P41 GM66326NIGMS NIH HHS U54 GM074901
6 · The paper itself

Abstract

We identified a functional domain (XlePABP2-TRP) of Xenopus laevis embryonic type II poly(A)-binding protein (XlePABP2). The NMR structure of XlePABP2-TRP revealed that the protein is a homodimer formed by the antiparallel association of beta-strands from the single RNA recognition motif (RRM) domain of each subunit. In each subunit of the homodimer, the canonical RNA recognition site is occluded by a polyproline motif. Upon poly(A) binding, XlePABP2-TRP undergoes a dimer-monomer transition that removes the polyproline motif from the RNA recognition site and allows it to be replaced by the adenosine nucleotides of poly(A). Our results provide high-resolution structural information concerning type II PABPs and an example of a single RRM domain protein that transitions from a homodimer to a monomer upon RNA binding. These findings advance our understanding of RRM domain regulation, poly(A) recognition, and are relevant to understanding how type II PABPs function in mRNA processing and human disease.

Indexed as

AnimalsBinding SitesModels, MolecularNuclear Magnetic Resonance, BiomolecularPoly APoly(A)-Binding Protein IIProtein ConformationProtein Structure, TertiaryRNAStructure-Activity RelationshipXenopusXenopus ProteinsPoly APoly(A)-Binding Protein IIRNAXenopus Proteins

Identifiers

PMID18824697
PMCPMC2563106
OpenAlexW2155671234

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.