EMD-24927

Single-particle
3.73 Å
EMD-24927 Deposition: 20/09/2021
Map released: 06/07/2022
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-24927

Leg region of a complex of IGF-I with the ectodomain of a hybrid insulin receptor / type 1 insulin-like growth factor receptor

EMD-24927

Single-particle
3.73 Å
EMD-24927 Deposition: 20/09/2021
Map released: 06/07/2022
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Homo sapiens
Sample: a complex of IGF-I with the ectodomain of a hybrid insulin receptor / type 1 insulin-like growth factor receptor
Fitted models: 7s8v (Avg. Q-score: 0.232)

Deposition Authors: Xu Y, Lawrence MC
How insulin-like growth factor I binds to a hybrid insulin receptor type 1 insulin-like growth factor receptor.
Xu Y, Margetts MB, Venugopal H , Menting JG, Kirk NS , Croll TI, Delaine C, Forbes BE , Lawrence MC
(2022) Structure , 30 , 1098 - 1108.e6
PUBMED: 35660159
DOI: doi:10.1016/j.str.2022.05.007
ISSN: 0969-2126
ASTM: STRUE6
Abstract:
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.