Evidence map›Paper›PMID 34419446›Full record

ArticleThe Journal of biological chemistry2021

Structural delineation and phase-dependent activation of the costimulatory CD27:CD70 complex.

Weifeng Liu, Zachary Maben, Carole Wang, Kevin C Lindquist, Manqing Li, Vinayak Rayannavar, Ilsel Lopez Armenta, Andrew Nager, Edward Pascua, Pawel K Dominik and 6 more

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

21 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
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  9. CD70 recruitment to the immunological synapse is dependent on CD20 in B cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  16. CD27 on human memory B cells-more than just a surface marker.Clinical and experimental immunology · 2023
    Review
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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

16 authors at 1 institution in 1 country.

Weifeng LiuPfizer, Inc, La Jolla, California, USA.
Zachary MabenPfizer, Inc, Cambridge, Massachusetts, USA.
Carole WangPfizer, Inc, La Jolla, California, USA.
Kevin C LindquistPfizer, Inc, La Jolla, California, USA.
Manqing LiPfizer, Inc, La Jolla, California, USA.
Vinayak RayannavarPfizer, Inc, La Jolla, California, USA.
Ilsel Lopez ArmentaPfizer, Inc, La Jolla, California, USA.
Andrew NagerPfizer, Inc, La Jolla, California, USA.
Edward PascuaPfizer, Inc, La Jolla, California, USA.
Pawel K DominikPfizer, Inc, La Jolla, California, USA.
David OyenPfizer, Inc, La Jolla, California, USA.
Hui WangPfizer, Inc, La Jolla, California, USA.
Rachel Carson RoachPfizer, Inc, La Jolla, California, USA.
Corey M AllanPfizer, Inc, La Jolla, California, USA.
Lidia MosyakPfizer, Inc, Cambridge, Massachusetts, USA. Electronic address: Lidia.Mosyak@pfizer.com.
Javier Chaparro-RiggersPfizer, Inc, La Jolla, California, USA. Electronic address: javier.chaparro-riggers@pfizer.com.
Pfizer (United States) · US

Funding

CIHR
6 · The paper itself

Abstract

CD27 is a tumor necrosis factor (TNF) receptor, which stimulates lymphocytes and promotes their differentiation upon activation by TNF ligand CD70. Activation of the CD27 receptor provides a costimulatory signal to promote T cell, B cell, and NK cell activity to facilitate antitumor and anti-infection immunity. Aberrant increased and focused expression of CD70 on many tumor cells renders CD70 an attractive therapeutic target for direct tumor killing. However, despite their use as drug targets to treat cancers, the molecular basis and atomic details of CD27 and CD70 interaction remain elusive. Here we report the crystal structure of human CD27 in complex with human CD70. Analysis of our structure shows that CD70 adopts a classical TNF ligand homotrimeric assembly to engage CD27 receptors in a 3:3 stoichiometry. By combining structural and rational mutagenesis data with reported disease-correlated mutations, we identified the key amino acid residues of CD27 and CD70 that control this interaction. We also report increased potency for plate-bound CD70 constructs compared with solution-phase ligand in a functional activity to stimulate T-cells in vitro. These findings offer new mechanistic insight into this critical costimulatory interaction.

Indexed as

CD27 LigandCrystallography, X-RayHumansMultiprotein ComplexesProtein Structure, QuaternaryT-LymphocytesTumor Necrosis Factor Receptor Superfamily, Member 7CD27 LigandCD70 protein, humanMultiprotein ComplexesTumor Necrosis Factor Receptor Superfamily, Member 7cell surface receptorcrystal structureprotein–protein interactionstructure–functiontumor necrosis factor (TNF)

Identifiers

PMID34419446
PMCPMC8484739
OpenAlexW3195452533

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.