Evidence map›Paper›PMID 12234919›Full record

ArticleThe EMBO journal2002

Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain.

Gerwald Jogl, Yang Shen, Damara Gebauer, Jiang Li, Katja Wiegmann, Hamid Kashkar, Martin Krönke, Liang Tong

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

41 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Spectrum ofJournal of medical genetics · 2024
    Review
  3. Article
  4. Review
  5. Review
  6. The evolving biology of cross-presentation.Seminars in immunology · 2023
    Review
  7. Dendritic cells in cancer immunology.Cellular & molecular immunology · 2022
    Review
  8. Article
  9. Article
  10. Genetic Analyses of Amphotericin B Susceptibility inJournal of fungi (Basel, Switzerland) · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. LRBA in the endomembrane system.Colombia medica (Cali, Colombia) · 2018
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

8 authors at 1 institution in 1 country.

Gerwald JoglDepartment of Biological Sciences, Columbia University, New York, NY 10027, USA.
Yang Shen
Damara Gebauer
Jiang Li
Katja Wiegmann
Hamid Kashkar
Martin Krönke
Liang Tong
Columbia University · US

Funding

Structural biology of BEACH-containing proteinsR01GM066753 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2003 to 2006
$1.1M
NIGMS NIH HHS GM066753NIGMS NIH HHS R01 GM066753
6 · The paper itself

Abstract

The BEACH domain is highly conserved in a large family of eukaryotic proteins, and is crucial for their functions in vesicle trafficking, membrane dynamics and receptor signaling. However, it does not share any sequence homology with other proteins. Here we report the crystal structure at 2.9 A resolution of the BEACH domain of human neurobeachin. It shows that the BEACH domain has a new and unusual polypeptide backbone fold, as the peptide segments in its core do not assume regular secondary structures. Unexpectedly, the structure also reveals that the BEACH domain is in extensive association with a novel, weakly conserved pleckstrin-homology (PH) domain. Consistent with the structural analysis, biochemical studies show that the PH and BEACH domains have strong interactions, suggesting they may function as a single unit. Functional studies in intact cells demonstrate the requirement of both the PH and the BEACH domains for activity. A prominent groove at the interface between the two domains may be used to recruit their binding partners.

Indexed as

Protein Structure, TertiaryAmino Acid SequenceAnimalsBinding SitesCarrier ProteinsChediak-Higashi SyndromeCrystallography, X-RayHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceModels, MolecularMolecular Sequence DataNerve Tissue ProteinsProtein BindingProteinsCarrier ProteinsIntracellular Signaling Peptides and ProteinsMembrane ProteinsNBEA protein, humanNbea protein, mouseNerve Tissue ProteinsNSMAF protein, humanNsmaf protein, mouseProteinsRecombinant Fusion Proteins

Identifiers

PMID12234919
PMCPMC126298
OpenAlexW2129001359

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.