6KRZ

Crystal structure of the human adiponectin receptor 1 D208A mutant

6KRZ の概要

• エントリーDOI: 10.2210/pdb6krz/pdb
• 分子名称: Adiponectin receptor protein 1, The heavy chain variable domain (Antibody), The light chain variable domain (Antibody), ... (8 entities in total)
• 機能のキーワード: membrane protein, membrane protein-immune system complex, membrane protein/immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 181174.96

構造登録者

Tanabe, H.,Fujii, Y.,Okada-Iwabu, M.,Iwabu, M.,Yamauchi, T.,Kadowaki, T.,Yokoyama, S. (登録日: 2019-08-22, 公開日: 2020-08-19, 最終更新日: 2024-11-20)

主引用文献

Tanabe, H.,Fujii, Y.,Okada-Iwabu, M.,Iwabu, M.,Kano, K.,Kawana, H.,Hato, M.,Nakamura, Y.,Terada, T.,Kimura-Someya, T.,Shirouzu, M.,Kawano, Y.,Yamamoto, M.,Aoki, J.,Yamauchi, T.,Kadowaki, T.,Yokoyama, S.
Human adiponectin receptor AdipoR1 assumes closed and open structures.
Commun Biol, 3:446-446, 2020

PubMed Abstract: The human adiponectin receptors, AdipoR1 and AdipoR2, are key anti-diabetic molecules. We previously reported the crystal structures of human AdipoR1 and AdipoR2, revealing that their seven transmembrane helices form an internal closed cavity (the closed form). In this study, we determined the crystal structure of the D208A variant AdipoR1, which is fully active with respect to the major downstream signaling. Among the three molecules in the asymmetric unit, two assume the closed form, and the other adopts the open form with large openings in the internal cavity. Between the closed- and open-form structures, helices IV and V are tilted with their intracellular ends shifted by about 4 and 11 Å, respectively. Furthermore, we reanalyzed our previous wild-type AdipoR1 diffraction data, and determined a 44:56 mixture of the closed and open forms, respectively. Thus, we have clarified the closed-open interconversion of AdipoR1, which may be relevant to its functional mechanism(s).

PubMed: 32796916
DOI: 10.1038/s42003-020-01160-4

実験手法

X-RAY DIFFRACTION (3.05 Å)