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6JK8

Cryo-EM structure of the full-length human IGF-1R in complex with insulin

Summary for 6JK8
Entry DOI10.2210/pdb6jk8/pdb
EMDB information9838
DescriptorInsulin-like growth factor 1 receptor, Insulin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
Functional Keywordshuman type 1 insulin-like growth factor receptor; insulin, signaling protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight337682.20
Authors
Zhang, X.,Yu, D.,Wang, T. (deposition date: 2019-02-27, release date: 2020-03-04, Last modification date: 2024-11-06)
Primary citationZhang, X.,Yu, D.,Sun, J.,Wu, Y.,Gong, J.,Li, X.,Liu, L.,Liu, S.,Liu, J.,Wu, Y.,Li, D.,Ma, Y.,Han, X.,Zhu, Y.,Wu, Z.,Wang, Y.,Ouyang, Q.,Wang, T.
Visualization of Ligand-Bound Ectodomain Assembly in the Full-Length Human IGF-1 Receptor by Cryo-EM Single-Particle Analysis.
Structure, 28:555-561.e4, 2020
Cited by
PubMed Abstract: Tyrosine kinase receptor of insulin-like growth factor 1 receptor (IGF-1R) and insulin receptor (IR) bind to hormones, such as insulin, IGF-1, and IGF-2, and transduces the signals across the cell membrane. However, the complete structure of the receptor and the signal transduction mechanism remains unclear. Here, we report the cryo-EM structure of the ligand-bound ectodomain in the full-length human IGF-1R. We reconstructed the IGF-1R/insulin complex at 4.7 Å and the IGF-1R/IGF-1 complex at 7.7 Å. Our structures reveal that only one insulin or one IGF-1 molecule binds to and activates the full-length human IGF-1R receptor.
PubMed: 32275863
DOI: 10.1016/j.str.2020.03.007
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (5 Å)
Structure validation

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