Evidence map›Paper›PMID 22308406›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Structural reorganization of the interleukin-7 signaling complex.

Craig A McElroy, Paul J Holland, Peng Zhao, Jae-Min Lim, Lance Wells, Edward Eisenstein, Scott T R Walsh

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

33 citing papers in PubMed, 63 citations in OpenAlex.

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  19. IL-7 Induces an Epitope Masking ofMediators of inflammation · 2017
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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 4 institutions in 3 countries.

Craig A McElroyBattelle Biomedical Research Center, Columbus, OH 43201, USA.
Paul J Holland
Peng Zhao
Jae-Min Lim
Lance Wells
Edward Eisenstein
Scott T R Walsh
University of Georgia · USInstitute for Bioscience and Biotechnology ResearchBattelle · USBioengineering Center · RU

Funding

ZINC DEFICIENCY &PROTEIN EXPRESSION IN RAT OLFACTORY BULBSP41RR018502 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI AZADI, PARASTOO · 2003 to 2011
$13.1M
Molecular Recognition Studies of the Interleukin-7 PathwayR01AI072142 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI WALSH, SCOTT T · 2008 to 2012
$1.6M
Molecular Recognition Studies of the Interleukin-7 PathwayR56AI072142 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI WALSH, SCOTT T · 2013 to 2013
$357k
NCRR NIH HHS P41 RR018502NCRR NIH HHS P41RR018502NIAID NIH HHS AI72142NIAID NIH HHS R01 AI072142NIAID NIH HHS R56 AI072142
6 · The paper itself

Abstract

We report here an unliganded receptor structure in the common gamma-chain (γ(c)) family of receptors and cytokines. The crystal structure of the unliganded form of the interleukin-7 alpha receptor (IL-7Rα) extracellular domain (ECD) at 2.15 Å resolution reveals a homodimer forming an "X" geometry looking down onto the cell surface with the C termini of the two chains separated by 110 Å and the dimer interface comprising residues critical for IL-7 binding. Further biophysical studies indicate a weak association of the IL-7Rα ECDs but a stronger association between the γ(c)/IL-7Rα ECDs, similar to previous studies of the full-length receptors on CD4(+) T cells. Based on these and previous results, we propose a molecular mechanism detailing the progression from the inactive IL-7Rα homodimer and IL-7Rα-γ(c) heterodimer to the active IL-7-IL-7Rα-γ(c) ternary complex whereby the two receptors undergo at least a 90° rotation away from the cell surface, moving the C termini of IL-7Rα and γ(c) from a distance of 110 Å to less than 30 Å at the cell surface. This molecular mechanism can be used to explain recently discovered IL-7- and γ(c)-independent gain-of-function mutations in IL-7Rα from B- and T-cell acute lymphoblastic leukemia patients. The mechanism may also be applicable to other γ(c) receptors that form inactive homodimers and heterodimers independent of their cytokines.

Indexed as

Signal TransductionDimerizationInterleukin-7LigandsProtein BindingProtein ConformationX-Ray DiffractionInterleukin-7Ligands

Identifiers

PMID22308406
PMCPMC3289338
OpenAlexW2096679660

What OpenQuestion holds

Textmetadata
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.