Evidence map›Paper›PMID 18621724›Full record

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

Solution structure of the U2 snRNP protein Rds3p reveals a knotted zinc-finger motif.

Anne-Marie M van Roon, Nikolaus M Loening, Eiji Obayashi, Ji-Chun Yang, Andrew J Newman, Helena Hernández, Kiyoshi Nagai, David Neuhaus

Open access · greenAbstract read
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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  5. Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019
    Review
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  17. A Stevedore's protein knot.PLoS computational biology · 2010
    Article
  18. Article
  19. Review
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

8 authors at 2 institutions in 2 countries.

Anne-Marie M van RoonMedical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, United Kingdom.
Nikolaus M Loening
Eiji Obayashi
Ji-Chun Yang
Andrew J Newman
Helena Hernández
Kiyoshi Nagai
David Neuhaus
Medical Research Council · GBMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105178934Medical Research Council MC_U105184285Medical Research Council MC_U105184330Wellcome Trust
6 · The paper itself

Abstract

Rds3p, a component of the U2 snRNP subcomplex SF3b, is essential for pre-mRNA splicing and is extremely well conserved in all eukaryotic species. We report here the solution structure of Rds3p, which reveals an unusual knotted fold unrelated to previously known knotted proteins. Rds3p has a triangular shape with a GATA-like zinc finger at each vertex. Pairs of cysteines contributing to each finger are arranged nonsequentially in a permuted arrangement reminiscent of domain-swapping but which here involves segments of subdomains within a single chain. We suggest that the structure arose through a process of segment swapping after gene duplication. The fingers are connected through beta-strands and loops, forming an overall topology strongly resembling a "triquetra knot." The conservation and surface properties of Rds3p suggest that it functions as a platform for protein assembly within the multiprotein SF3b complex of U2 snRNP. The recombinant protein used for structure determination is biologically active, as it restores splicing activity in a yeast splicing extract depleted of native Rds3p.

Indexed as

Zinc FingersCarrier ProteinsCysteineProtein ConformationRibonucleoprotein, U2 Small NuclearSaccharomyces cerevisiae ProteinsSolutionsCarrier ProteinsCysteineRDS3 protein, S cerevisiaeRibonucleoprotein, U2 Small NuclearSaccharomyces cerevisiae ProteinsSolutions

Identifiers

PMID18621724
PMCPMC2474504
OpenAlexW2046821309

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.