Evidence map›Paper›PMID 21559424›Full record

ArticlePloS one2011

LILRA3 binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1/LILRB2: structural evidence.

Myongchol Ryu, Yong Chen, Jianxun Qi, Jun Liu, Zheng Fan, Gol Nam, Yi Shi, Hao Cheng, George F Gao

Registry-linked trialOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT05915676 (Frequency Assessment of Leukocyte Immunoglobulin-like Receptors A3 In Ankylosing Spondylitis And Axial Psoriatic Arthritis Patients), which is not on this map. Cited by 29 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 17% 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.

NCT05915676 unknown statusnot on this mapstarted 2023, after this paper: background citation

Frequency Assessment of Leukocyte Immunoglobulin-like Receptors A3 In Ankylosing Spondylitis And Axial Psoriatic Arthritis Patients

TypeobservationalSponsorAssiut UniversityRan2023 to 2024Enrolled100ConditionsAutoimmune DiseasesArmsLeukocyte Immunoglobulin-like receptors A3
3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 1 synthesis or guideline pooled it, 38 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Frontiers in immunology · 2025
    Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Frequencies of theFrontiers in genetics · 2019
    Article
  14. Genetic determinants and an epistasis ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  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

9 authors at 3 institutions in 2 countries.

Myongchol RyuCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Yong Chen
Jianxun Qi
Jun Liu
Zheng Fan
Gol Nam
Yi Shi
Hao Cheng
George F Gao
Institute of Microbiology · CNUniversity of Chinese Academy of Sciences · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structurally, Group 1 LILR (Leukocyte Immunoglobulin (Ig)-Like Receptor, also known as Ig-like transcripts, ILT; Leukocyte Ig-like receptor, LIR; and CD85) members are very similar in terms of the HLAIs (human leukocyte antigen class I molecules) binding region and were hypothesized that they all bind to HLAIs. As one of the Group 1 LILRs, LILRA3 is the only secretory LILR and may greatly control the inhibitory immune response induced by LILRB1, LILRB2, and other HLA-binding LILR molecules like LILRA1. Nevertheless, little was known about the binding of LILRA3 to HLAIs. In this report, we present the crystal structure of the LILRA3 domain 1 (D1) and evaluate the D1 and D1D2 (domain 1 and domain 2) binding to classical and non-classical HLAIs using BIAcore® surface plasmon resonance analysis (SPR). We found that LILRA3 binds both classical HLA-A*0201 and non-classical HLA-G1 but with reduced affinities compared to either LILRB1 or LILRB2. The polymorphic amino acids and the LILRA3 D1 structure support this notion.

Indexed as

Amino Acid SequenceAntigens, CDCrystallography, X-RayHistocompatibility Antigens Class IHumansHydrogen BondingImmune SystemKineticsLeukocyte Immunoglobulin-like Receptor B1Membrane GlycoproteinsModels, MolecularMolecular ConformationMolecular Sequence DataProtein BindingProtein Structure, TertiaryReceptors, ImmunologicAntigens, CDHistocompatibility Antigens Class ILeukocyte Immunoglobulin-like Receptor B1LILRA3 protein, humanLILRB1 protein, humanLILRB2 protein, humanMembrane GlycoproteinsReceptors, Immunologic

Identifiers

PMID21559424
PMCPMC3084784
OpenAlexW2074849310

What OpenQuestion holds

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Registered trials

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.