Evidence map›Paper›PMID 16498413›Full record

ArticleThe EMBO journal2006

Structural and functional insights into the B30.2/SPRY domain.

Jae-Sung Woo, Joon-Hyuk Imm, Chang-Ki Min, Kyung-Jin Kim, Sun-Shin Cha, Byung-Ha Oh

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
11.0field-weighted citation impact, top 1% 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

79 citing papers in PubMed, 157 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Is MG53 a potential therapeutic target for cancer?Frontiers in endocrinology · 2023
    Review
  11. Genetic diagnosis for adult patients at a genetic clinic.Cold Spring Harbor molecular case studies · 2022
    Article
  12. Review
  13. Review
  14. Crystal structure of the SPRY domain of human SPSB2 in the apo state.Acta crystallographica. Section F, Structural biology communications · 2019
    Article
  15. Article
  16. Review
  17. Sequence analysis of the cDNA encoding for SpCTx: a lethal factor from scorpionfish venom (The journal of venomous animals and toxins including tropical diseases · 2018
    Article
  18. Ubiquitin enzymes in the regulation of immune responses.Critical reviews in biochemistry and molecular biology · 2017
    Review
  19. Review
  20. Article

19 more citing papers are in PubMed but not listed here.

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

6 authors at 1 institution in 1 country.

Jae-Sung WooDivision of Molecular and Life Sciences, Department of Life Sciences, Center for Biomolecular Recognition, Pohang University of Science and Technology, Pohang, Kyungbuk, Korea.
Joon-Hyuk Imm
Chang-Ki Min
Kyung-Jin Kim
Sun-Shin Cha
Byung-Ha Oh
Pohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The B30.2/SPRY domain is present in approximately 700 eukaryotic (approximately 150 human) proteins, including medically important proteins such as TRIM5alpha and Pyrin. Nonetheless, the functional role of this modular domain remained unclear. Here, we report the crystal structure of an SPRY-SOCS box family protein GUSTAVUS in complex with Elongins B and C, revealing a highly distorted two-layered beta-sandwich core structure of its B30.2/SPRY domain. Ensuing studies identified one end of the beta-sandwich as the surface interacting with an RNA helicase VASA with a 40 nM dissociation constant. The sequence variation in TRIM5alpha responsible for HIV-1 restriction and most of the mutations in Pyrin causing familial Mediterranean fever map on this surface, implicating the corresponding region in many B30.2/SPRY domains as the ligand-binding site. The amino acids lining the binding surface are highly variable among the B30.2/SPRY domains, suggesting that these domains are protein-interacting modules, which recognize a specific individual partner protein rather than a consensus sequence motif.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsBinding SitesCarrier ProteinsCytoskeletal ProteinsDEAD-box RNA HelicasesDrosophila ProteinsElonginLigandsModels, MolecularMolecular Sequence DataMutationProtein BindingProtein ConformationProtein FoldingCarrier ProteinsCytoskeletal ProteinsDEAD-box RNA HelicasesDrosophila ProteinsElongingus protein, DrosophilaLigandsMEFV protein, humanPyrinRNA HelicasesTranscription Factorsvas protein, Drosophila

Identifiers

PMID16498413
PMCPMC1422157
OpenAlexW2113818355

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.