Evidence map›Paper›PMID 21240269›Full record

ArticleNature structural & molecular biology2011

Crystal structure of autotaxin and insight into GPCR activation by lipid mediators.

Hiroshi Nishimasu, Shinichi Okudaira, Kotaro Hama, Emiko Mihara, Naoshi Dohmae, Asuka Inoue, Ryuichiro Ishitani, Junichi Takagi, Junken Aoki, Osamu Nureki

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Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing papers in PubMed
11.7field-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

114 citing papers in PubMed, 246 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Lysophosphatidic acid signaling via LPAJournal of neurochemistry · 2022
    Article
  11. Article
  12. Article
  13. Designing Dual Inhibitors of Autotaxin-LPAR GPCR Axis.Molecules (Basel, Switzerland) · 2022
    Review
  14. World journal of gastrointestinal oncology · 2022
    Review
  15. Article
  16. Article
  17. Design and Development of Autotaxin Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 1 country.

Hiroshi NishimasuDepartment of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Tokyo, Japan.
Shinichi Okudaira
Kotaro Hama
Emiko Mihara
Naoshi Dohmae
Asuka Inoue
Ryuichiro Ishitani
Junichi Takagi
Junken Aoki
Osamu Nureki
Tohoku University · JPThe University of Tokyo · JPProtein Research Foundation · JPRIKEN · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autotaxin (ATX, also known as Enpp2) is a secreted lysophospholipase D that hydrolyzes lysophosphatidylcholine to generate lysophosphatidic acid (LPA), a lipid mediator that activates G protein-coupled receptors to evoke various cellular responses. Here, we report the crystal structures of mouse ATX alone and in complex with LPAs with different acyl-chain lengths and saturations. These structures reveal that the multidomain architecture helps to maintain the structural rigidity of the lipid-binding pocket, which accommodates the respective LPA molecules in distinct conformations. They indicate that a loop region in the catalytic domain is a major determinant for the substrate specificity of the Enpp family enzymes. Furthermore, along with biochemical and biological data, these structures suggest that the produced LPAs are delivered from the active site to cognate G protein-coupled receptors through a hydrophobic channel.

Indexed as

Amino Acid SequenceAnimalsBinding SitesCell LineCrystallography, X-RayHumansHydrophobic and Hydrophilic InteractionsLysophospholipase DLysophospholipidsMiceModels, MolecularMolecular Sequence DataMultienzyme ComplexesPhosphodiesterase IPhosphoric Diester HydrolasesProtein Conformationlysophosphatidic acidLysophospholipase DLysophospholipidsMultienzyme ComplexesPhosphodiesterase IPhosphoric Diester HydrolasesPyrophosphatasesReceptors, G-Protein-Coupled

Identifiers

PMID21240269
OpenAlexW2166617029

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.