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Updated: Sep 6, 2025
Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity
Published on: January 15, 2014
Cryo-EM studies of the apo states of human IGF1R
Xi Zhang1, Cang Wu2, Tianzi Wei3
1Department of Gastroenterology, The First Affiliated Hospital of Shenzhen University, Shenzhen People's Second Hospital, Shenzhen, 518000, Guangdong, China; Institute of Synthetic Biology, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, 518055, Guangdong, China; Cryo-EM Centre, Southern University of Science and Technology, Shenzhen, 518055, Guangdong, China.
Abstract:
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.
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