Cryo-EM studies of the apo states of human IGF1R.

Xi Zhang, Cang Wu, Tianzi Wei, Yi Lu, Chuang Liu, Jian Zhang

Biochemical and biophysical research communications 2022 Aug 27

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IGF1R plays an important role in regulating cellular metabolism and growth. As a single transmembrane protein, its structure is flexible. Although previous studies revealed some structures of IGF1R, the cryo-EM apo structures of the receptor have never been reported. Herein, we reported four distinct cryo-EM structures that reveal the apo states of IGF1R. These conformations were classified as "Resting states" and "Active states", according to the orientation of α-CT helices and structural symmetry. In addition, a "Ligand-pocket" was formed in the active conformations, which presented a new view of conformational changes of apo-IGF1R. These results suggest a new dynamic change model to show the details of why and how ligands can bind to IGF1R. Copyright © 2022 Elsevier Inc. All rights reserved.

Citation

Xi Zhang, Cang Wu, Tianzi Wei, Yi Lu, Chuang Liu, Jian Zhang. Cryo-EM studies of the apo states of human IGF1R. Biochemical and biophysical research communications. 2022 Aug 27;618:148-152