Evidence map›Paper›PMID 18547526›Full record

ArticleStructure (London, England : 1993)2008

Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain.

Ioannis Vakonakis, Tobias Langenhan, Simone Prömel, Andreas Russ, Iain D Campbell

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Latrophilin's Social Protein Network.Frontiers in neuroscience · 2019
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Structural basis of latrophilin-FLRT interaction.Structure (London, England : 1993) · 2015
    Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Folding helical proteins in explicit solvent using dihedral-biased tempering.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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

5 authors at 1 institution in 1 country.

Ioannis VakonakisDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, United Kingdom. ioannis.vakonakis@bioch.ox.ac.uk
Tobias Langenhan
Simone Prömel
Andreas Russ
Iain D Campbell
University of Oxford · GB

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SASISEKHARAN, RAM · 2001 to 2010
$80.3M
NIGMS NIH HHS U54 GM062116Wellcome Trust
6 · The paper itself

Abstract

Latrophilin-1 (Lat-1), a target receptor for alpha-Latrotoxin, is a putative G protein-coupled receptor implicated in synaptic function. The extracellular portion of Lat-1 contains a rhamnose binding lectin (RBL)-like domain of unknown structure. RBL domains, first isolated from the eggs of marine species, are also found in the ectodomains of other metazoan transmembrane proteins, including a recently discovered coreceptor of the neuronal axon guidance molecule SLT-1/Slit. Here, we describe a structure of this domain from the mouse Lat-1. RBL adopts a unique alpha/beta fold with long structured loops important for monosaccharide recognition, as shown in the structure of a complex with L-rhamnose. Sequence alignments and mutagenesis show that residues important for carbohydrate binding are often absent in other receptor-attached examples of RBL, including the SLT-1/Slit coreceptor. We postulate that this domain class facilitates direct protein-protein interactions in many transmembrane receptors.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsCarbohydratesLectinsMiceModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Structure, TertiaryReceptors, G-Protein-CoupledReceptors, PeptideRhamnoseSequence Homology, Amino AcidSolutionsAdgrl1 protein, mouseCarbohydratesLectinsReceptors, G-Protein-CoupledReceptors, PeptideRhamnoseSolutions

Identifiers

PMID18547526
PMCPMC2430599
OpenAlexW2059860628

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.