Evidence map›Paper›PMID 32459985›Full record

ArticleStructure (London, England : 1993)2020

How IGF-II Binds to the Human Type 1 Insulin-like Growth Factor Receptor.

Yibin Xu, Nicholas S Kirk, Hariprasad Venugopal, Mai B Margetts, Tristan I Croll, Jarrod J Sandow, Andrew I Webb, Carlie A Delaine, Briony E Forbes, Michael C Lawrence

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

38 citing papers in PubMed, 52 citations in OpenAlex.

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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

10 authors at 5 institutions in 2 countries.

Yibin XuWalter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; Department of Medical Biology, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Parkville, VIC 3050, Australia.
Nicholas S KirkWalter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; Department of Medical Biology, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Parkville, VIC 3050, Australia.
Hariprasad VenugopalRamaciotti Centre for Cryo-Electron Microscopy, Monash University, Clayton, VIC 3800, Australia.
Mai B MargettsWalter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia.
Tristan I CrollCambridge Institute for Medical Research, University of Cambridge, Wellcome Trust/MRC Building, Cambridge CB2 0XY, UK.
Jarrod J SandowWalter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; Department of Medical Biology, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Parkville, VIC 3050, Australia.
Andrew I WebbWalter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; Department of Medical Biology, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Parkville, VIC 3050, Australia.
Carlie A DelaineFlinders Health and Medical Research Institute, College of Medicine and Public Health, Flinders University of South Australia, Bedford Park, SA 5042, Australia.
Briony E ForbesFlinders Health and Medical Research Institute, College of Medicine and Public Health, Flinders University of South Australia, Bedford Park, SA 5042, Australia.
Michael C LawrenceWalter and Eliza Hall Institute of Medical Research, Parkville, VIC 3052, Australia; Department of Medical Biology, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Parkville, VIC 3050, Australia. Electronic address: lawrence@wehi.edu.au.
University of Melbourne · AUWalter and Eliza Hall Institute of Medical Research · AUFlinders University · AUMonash University · AUWellcome Trust · GB

Funding

ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
NIGMS NIH HHS R01 GM129325Wellcome Trust 209407/Z/17/Z
6 · The paper itself

Abstract

Human type 1 insulin-like growth factor receptor (IGF-1R) signals chiefly in response to the binding of insulin-like growth factor I. Relatively little is known about the role of insulin-like growth factor II signaling via IGF-1R, despite the affinity of insulin-like growth factor II for IGF-1R being within an order of magnitude of that of insulin-like growth factor I. Here, we describe the cryoelectron microscopy structure of insulin-like growth factor II bound to a leucine-zipper-stabilized IGF-1R ectodomain, determined in two conformations to a maximum average resolution of 3.2 Å. The two conformations differ in the relative separation of their respective points of membrane entry, and comparison with the structure of insulin-like growth factor I bound to IGF-1R reveals long-suspected differences in the way in which the critical C domain of the respective growth factors interact with IGF-1R.

Indexed as

3T3 CellsAnimalsBinding SitesCHO CellsCricetinaeCricetulusCryoelectron MicroscopyHumansInsulin-Like Growth Factor IIMiceMolecular Docking SimulationProtein BindingReceptor, IGF Type 1Insulin-Like Growth Factor IIReceptor, IGF Type 1cryoelectron microscopyinsulin-like growth factor Iinsulin-like growth factor IIleucine zippersingle-particle 3D reconstructiontype 1 insulin-like growth factor receptor

Identifiers

PMID32459985
PMCPMC7343240
OpenAlexW3031309210

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.