How insulin-like growth factor I binds to a hybrid insulin receptor type 1 insulin-like growth factor receptor.

Cryoelectron Microscopy Cysteine Insulin / metabolism Insulin-Like Growth Factor I / metabolism Ligands Receptor, IGF Type 1 / chemistry Receptor, Insulin / chemistry Receptors, Somatomedin
cryo-electron microscopy hybrid receptor insulin receptor insulin-like growth factor I leucine zipper type 1 insulin-like growth factor receptor

Journal

Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697

Informations de publication

Date de publication:
04 08 2022
Historique:
received: 07 12 2021
revised: 11 04 2022
accepted: 10 05 2022
pubmed: 7 6 2022
medline: 10 8 2022
entrez: 6 6 2022
Statut: ppublish

Résumé

Monomers of the insulin receptor and type 1 insulin-like growth factor receptor (IGF-1R) can combine stochastically to form heterodimeric hybrid receptors. These hybrid receptors display ligand binding and signaling properties that differ from those of the homodimeric receptors. Here, we describe the cryoelectron microscopy structure of such a hybrid receptor in complex with insulin-like growth factor I (IGF-I). The structure (ca. 3.7 Å resolution) displays a single IGF-I ligand, bound in a similar fashion to that seen for IGFs in complex with IGF-1R. The IGF-I ligand engages the first leucine-rich-repeat domain and cysteine-rich region of the IGF-1R monomer (rather than those of the insulin receptor monomer), consistent with the determinants for IGF binding residing in the IGF-1R cysteine-rich region. The structure broadens our understanding of this receptor family and assists in delineating the key structural motifs involved in binding their respective ligands.

Identifiants

DOI: 10.1016/j.str.2022.05.007 PMID: 35660159 PMC: PMC9364964
pubmed: 35660159
pii: S0969-2126(22)00181-2
doi: 10.1016/j.str.2022.05.007
pmc: PMC9364964
pii:
doi:

Substances chimiques

Insulin 0
Ligands 0
Receptors, Somatomedin 0
Insulin-Like Growth Factor I 67763-96-6
Receptor, IGF Type 1 EC 2.7.10.1
Receptor, Insulin EC 2.7.10.1
Cysteine K848JZ4886

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

1098-1108.e6

Subventions

Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 209407/Z/17/Z
Pays : United Kingdom

Informations de copyright

Copyright © 2022 The Author(s). Published by Elsevier Ltd.. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests M.C.L.’s laboratory has a funded agreement with Eli Lilly and Company to conduct research not connected to this publication.

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Auteurs

Yibin Xu (Y)

WEHI, 1G Royal Parade, Parkville, VIC 3052, Australia; Department of Medical Biology, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Parkville, VIC 3050, Australia.

Mai B Margetts (MB)

WEHI, 1G Royal Parade, Parkville, VIC 3052, Australia.

Hari Venugopal (H)

Ramaciotti Centre for Cryo-Electron Microscopy, Monash University, Clayton, VIC 3800, Australia.

John G Menting (JG)

WEHI, 1G Royal Parade, Parkville, VIC 3052, Australia; Department of Medical Biology, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Parkville, VIC 3050, Australia.

Nicholas S Kirk (NS)

WEHI, 1G Royal Parade, Parkville, VIC 3052, Australia; Department of Medical Biology, Faculty of Medicine, Dentistry and Health Sciences, University of Melbourne, Parkville, VIC 3050, Australia.

Tristan I Croll (TI)

Cambridge Institute for Medical Research, University of Cambridge, Keith Peters Building, Cambridge CB2 0XY, UK.

Carlie Delaine (C)

Discipline of Medical Biochemistry, College of Medicine and Public Health, Flinders University of South Australia, Bedford Park, SA 5042, Australia.

Briony E Forbes (BE)

Discipline of Medical Biochemistry, College of Medicine and Public Health, Flinders University of South Australia, Bedford Park, SA 5042, Australia.

Michael C Lawrence (MC)

WEHI, 1G Royal Parade, 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.

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Classifications MeSH

Recherchemedicale.com › Techniques d'investigation › Microscopie électronique › Cryomicroscopie électronique › How insulin-like growth factor I binds to a...
Recherchemedicale.com › Acides aminés, peptides et protéines › Acides aminés › Acides aminés soufrés › Cystéine › How insulin-like growth factor I binds to a...
Recherchemedicale.com › Acides aminés, peptides et protéines › Peptides › Hormones peptidiques › Hormones pancréatiques › Insulines › Insuline › How insulin-like growth factor I binds to a...
Recherchemedicale.com › Facteurs biologiques › Protéines et peptides de signalisation intercellulaire › Somatomédines › Facteur de croissance IGF-I › How insulin-like growth factor I binds to a...
Recherchemedicale.com › Actions chimiques et utilisations › Utilisations spécialisées de produits chimiques › Produits chimiques de laboratoire › Ligands › How insulin-like growth factor I binds to a...
Recherchemedicale.com › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Récepteurs de surface cellulaire › Récepteurs peptidiques › Récepteur facteur croissance › Récepteurs des somatomédines › Récepteur IGF de type 1 › How insulin-like growth factor I binds to a...
Recherchemedicale.com › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Récepteurs de surface cellulaire › Récepteurs peptidiques › Récepteur hormone pancréatique › Récepteur à l'insuline › How insulin-like growth factor I binds to a...
Recherchemedicale.com › Acides aminés, peptides et protéines › Protéines › Protéines membranaires › Récepteurs de surface cellulaire › Récepteurs peptidiques › Récepteur facteur croissance › Récepteurs des somatomédines › How insulin-like growth factor I binds to a...