Evidence map›Paper›PMID 20561531›Full record

ArticleJournal of molecular biology2010

Structural basis for Par-4 recognition by the SPRY domain- and SOCS box-containing proteins SPSB1, SPSB2, and SPSB4.

Panagis Filippakopoulos, Andrew Low, Timothy D Sharpe, Jonas Uppenberg, Shenggen Yao, Zhihe Kuang, Pavel Savitsky, Rowena S Lewis, Sandra E Nicholson, Raymond S Norton and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

34 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. E3 Ligase Ligands for PROTACs: How They Were Found and How to Discover New Ones.SLAS discovery : advancing life sciences R & D · 2021
    Review
  9. Article
  10. Article
  11. Targeted protein degradation: expanding the toolbox.Nature reviews. Drug discovery · 2019
    Article
  12. Crystal structure of the SPRY domain of human SPSB2 in the apo state.Acta crystallographica. Section F, Structural biology communications · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. 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

11 authors at 3 institutions in 2 countries.

Panagis FilippakopoulosStructural Genomics Consortium, University of Oxford, Old Road Campus, Roosevelt Drive, Oxford OX3 7DQ, UK.
Andrew Low
Timothy D Sharpe
Jonas Uppenberg
Shenggen Yao
Zhihe Kuang
Pavel Savitsky
Rowena S Lewis
Sandra E Nicholson
Raymond S Norton
Alex N Bullock
Walter and Eliza Hall Institute of Medical Research · AUGenomics (United Kingdom) · GBUniversity of Oxford · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The mammalian SPRY domain- and SOCS box-containing proteins, SPSB1 to SPSB4, belong to the SOCS box family of E3 ubiquitin ligases. Substrate recognition sites for the SPRY domain are identified only for human Par-4 (ELNNNL) and for the Drosophila orthologue GUSTAVUS binding to the DEAD-box RNA helicase VASA (DINNNN). To further investigate this consensus motif, we determined the crystal structures of SPSB1, SPSB2, and SPSB4, as well as their binding modes and affinities for both Par-4 and VASA. Mutation of each of the three Asn residues in Par-4 abrogated binding to all three SPSB proteins, while changing EL to DI enhanced binding. By comparison to SPSB1 and SPSB4, the more divergent protein SPSB2 showed only weak binding to Par-4 and was hypersensitive to DI substitution. Par-4((59-77)) binding perturbed NMR resonances from a number of SPSB2 residues flanking the ELNNN binding site, including loop D, which binds the EL/DI sequence. Although interactions with the consensus peptide motif were conserved in all structures, flanking sites in SPSB2 were identified as sites of structural change. These structural changes limit high-affinity interactions for SPSB2 to aspartate-containing sequences, whereas SPSB1 and SPSB4 bind strongly to both Par-4 and VASA peptides.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsBinding SitesConsensus SequenceCrystallography, X-RayDEAD-box RNA HelicasesHumansMagnetic Resonance SpectroscopyMiceProtein BindingProtein ConformationReceptors, ThrombinSuppressor of Cytokine Signaling ProteinsDDX4 protein, humanDdx4 protein, mouseDEAD-box RNA Helicasesprotease-activated receptor 4Receptors, ThrombinSPSB2 protein, humanSSB-1 protein, mouseSuppressor of Cytokine Signaling Proteins

Identifiers

PMID20561531
PMCPMC2923778
OpenAlexW2161251896

What OpenQuestion holds

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LicenceCC BY
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.