6VWG

Head region of the open conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II.

Summary for 6VWG

• Entry DOI: 10.2210/pdb6vwg/pdb
• EMDB information: 21415 21416
• Descriptor: Leucine-zippered human type 1 insulin-like growth factor receptor ectodomain, Insulin-like growth factor II, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: type 1 insulin-like growth factor receptor, insulin-like growth factor ii, ectodomain receptor, tyrosine kinase, signaling protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 226243.79

Authors

Xu, Y.,Kirk, N.S.,Lawrence, M.C.,Croll, T.I. (deposition date: 2020-02-19, release date: 2020-05-13, Last modification date: 2024-10-09)

Primary citation

Xu, Y.,Kirk, N.S.,Venugopal, H.,Margetts, M.B.,Croll, T.I.,Sandow, J.J.,Webb, A.I.,Delaine, C.A.,Forbes, B.E.,Lawrence, M.C.
How IGF-II Binds to the Human Type 1 Insulin-like Growth Factor Receptor.
Structure, 28:786-798.e6, 2020

PubMed 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.

PubMed: 32459985
DOI: 10.1016/j.str.2020.05.002

Experimental method

ELECTRON MICROSCOPY (3.21 Å)