6VWI
Head region of the closed conformation of the human type 1 insulin-like growth factor receptor ectodomain in complex with human insulin-like growth factor II.
6VWI の概要
| エントリーDOI | 10.2210/pdb6vwi/pdb |
| EMDBエントリー | 21415 21416 21417 21418 |
| 分子名称 | 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) |
| 機能のキーワード | type 1 insulin-like growth factor receptor, insulin-like growth factor ii, ectodomain receptor, tyrosine kinase, signaling protein |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 226243.79 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 32459985DOI: 10.1016/j.str.2020.05.002 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.7 Å) |
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