Evidence map›Paper›PMID 31230945›Full record

ArticleStructure (London, England : 1993)2019

Structural Basis of CD160:HVEM Recognition.

Weifeng Liu, Sarah C Garrett, Elena V Fedorov, Udupi A Ramagopal, Scott J Garforth, Jeffrey B Bonanno, Steven C Almo

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.0field-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

27 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
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  3. Article
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  7. Proteomic Investigation of Immune Checkpoints and Some of Their Inhibitors.International journal of molecular sciences · 2024
    Review
  8. Effect ofInternational journal of molecular sciences · 2024
    Article
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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

7 authors at 1 institution in 1 country.

Weifeng LiuDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Sarah C GarrettDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Elena V FedorovDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Udupi A RamagopalDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Scott J GarforthDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Jeffrey B BonannoDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Steven C AlmoDepartment of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA; Department of Physiology and Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. Electronic address: steve.almo@einstein.yu.edu.
Albert Einstein College of Medicine · US

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI THOMAS E ROHAN · 1985 to 2026
$111.2M
X-RAY STRUCTURE OF RIFM PROTEIN FROM THE BIOSYNTHESIS PATHWAY OF THE ANSAMYCIN AP41RR012408 · NCRR · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI ORVILLE, ALLEN M · 1998 to 2011
$32.2M
Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
Macromolecular Crystallography at the National Synchrotron Light SourceP41GM103473 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI SWEET, ROBERT M · 2012 to 2013
$4.9M
An integrated X-ray data collection systemS10OD020068 · OD · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI ALMO, STEVEN C. · 2015 to 2015
$600k
NCI NIH HHS P30 CA013330NCRR NIH HHS P41 RR012408NIBIB NIH HHS P30 EB009998NIGMS NIH HHS P41 GM103473NIH HHS S10 OD020068
6 · The paper itself

Abstract

CD160 is a signaling molecule that interacts with herpes virus entry mediator (HVEM) and contributes to a wide range of immune responses, including T cell inhibition, natural killer cell activation, and mucosal immunity. GPI-anchored and transmembrane isoforms of CD160 share the same ectodomain responsible for HVEM engagement, which leads to bidirectional signaling. Despite the importance of the CD160:HVEM signaling axis and its therapeutic relevance, the structural and mechanistic basis underlying CD160-HVEM engagement has not been described. We report the crystal structures of the human CD160 extracellular domain and its complex with human HVEM. CD160 adopts a unique variation of the immunoglobulin fold and exists as a monomer in solution. The CD160:HVEM assembly exhibits a 1:1 stoichiometry and a binding interface similar to that observed in the BTLA:HVEM complex. Our work reveals the chemical and physical determinants underlying CD160:HVEM recognition and initiation of associated signaling processes.

Indexed as

Antigens, CDBinding SitesCrystallography, X-RayGPI-Linked ProteinsHEK293 CellsHumansModels, MolecularProtein BindingProtein Conformation, beta-StrandProtein DomainsProtein FoldingReceptors, ImmunologicReceptors, Tumor Necrosis Factor, Member 14Antigens, CDBTLA protein, humanCD160 protein, humanGPI-Linked ProteinsReceptors, ImmunologicReceptors, Tumor Necrosis Factor, Member 14TNFRSF14 protein, humanCD160 and HVEMIgSF and TNFRSF interactionsimmune regulationInteraction promiscuityintermolecular beta-sheetT cell costimulation and coinhibitionX-ray structures

Identifiers

PMID31230945
PMCPMC7477951
OpenAlexW2950388260

What OpenQuestion holds

Textmetadata
LicenceTDM
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.