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How IGF-II Binds to the Human Type 1 Insulin-like Growth Factor Receptor.
- Source :
-
Structure . Jul2020, Vol. 28 Issue 7, p786-786. 1p. - Publication Year :
- 2020
-
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. • Cryo-EM structure of IGF-II bound to leucine-zippered human IGF-1R ectodomain • IGF-II C domain interacts with receptor differently to that of IGF-I Insulin-like growth factors I and II differ in the length of their C domain, the segment that links growth factor B and A domains. Xu et al. show that the different 3D modes of C-domain engagement with type 1 insulin-like growth factor receptor align with their receptor affinity. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09692126
- Volume :
- 28
- Issue :
- 7
- Database :
- Academic Search Index
- Journal :
- Structure
- Publication Type :
- Academic Journal
- Accession number :
- 144318354
- Full Text :
- https://doi.org/10.1016/j.str.2020.05.002