Evidence map›Paper›PMID 24465760›Full record

ArticlePloS one2014

Crystal structure of the lamprey variable lymphocyte receptor C reveals an unusual feature in its N-terminal capping module.

Ryo Kanda, Yoichi Sutoh, Jun Kasamatsu, Katsumi Maenaka, Masanori Kasahara, Toyoyuki Ose

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Bos taurus ultralong CDR H3 antibodies.Current opinion in structural biology · 2016
    Review
  8. Article
  9. Article
  10. Selection of the lamprey VLRC antigen receptor repertoire.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  11. Genomic donor cassette sharing during VLRA and VLRC assembly in jawless vertebrates.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
  13. 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

6 authors at 1 institution in 1 country.

Ryo KandaGraduate School of Life Sciences, Hokkaido University, Sapporo, Japan.
Yoichi SutohDepartment of Pathology, Hokkaido University Graduate School of Medicine, Sapporo, Japan.
Jun KasamatsuDepartment of Pathology, Hokkaido University Graduate School of Medicine, Sapporo, Japan.
Katsumi MaenakaFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Masanori KasaharaDepartment of Pathology, Hokkaido University Graduate School of Medicine, Sapporo, Japan.
Toyoyuki OseFaculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Hokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Jawless vertebrates represented by lampreys and hagfish use variable lymphocyte receptors (VLRs) as antigen receptors to mount adaptive immune responses. VLRs generate diversity that is comparable to immunoglobulins and T-cell receptors by a gene conversion-like mechanism, which is mediated by cytosine deaminases. Currently, three types of VLRs, VLRA, VLRB, and VLRC, have been identified in lampreys. Crystal structures of VLRA and VLRB in complex with antigens have been reported recently, but no structural information is available for VLRC. Here, we present the first crystal structure of VLRC from the Japanese lamprey (Lethenteron japonicum). Similar to VLRA and VLRB, VLRC forms a typical horseshoe-like solenoid structure with a variable concave surface. Strikingly, its N-terminal cap has a long loop with limited sequence variability that protrudes toward the concave surface, which is the putative antigen-binding surface. Furthermore, as predicted previously, its C-terminal cap lacks a highly variable protruding loop that plays an important role in antigen recognition by lamprey VLRA and VLRB. Recent work suggests that VLRC+ lymphocytes in jawless vertebrates might be akin to γδ T cells in jawed vertebrates. Structural features of lamprey VLRC described here suggest that it may recognize antigens in a unique manner.

Indexed as

LampreysAmino Acid SequenceAnimalsBinding SitesCrystallography, X-RayCystineFish ProteinsModels, MolecularMolecular Sequence DataProtein Structure, SecondaryProtein Structure, TertiaryReceptors, AntigenStructural Homology, ProteinCystineFish ProteinsReceptors, Antigen

Identifiers

PMID24465760
PMCPMC3900441
OpenAlexW2081071461

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.