Human adiponectin receptor AdipoR1 assumes closed and open structures View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2020-08-14

AUTHORS

Hiroaki Tanabe, Yoshifumi Fujii, Miki Okada-Iwabu, Masato Iwabu, Kuniyuki Kano, Hiroki Kawana, Masakatsu Hato, Yoshihiro Nakamura, Takaho Terada, Tomomi Kimura-Someya, Mikako Shirouzu, Yoshiaki Kawano, Masaki Yamamoto, Junken Aoki, Toshimasa Yamauchi, Takashi Kadowaki, Shigeyuki Yokoyama

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). More... »

PAGES

446

Journal

TITLE

Communications Biology

ISSUE

1

VOLUME

3

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s42003-020-01160-4

DOI

http://dx.doi.org/10.1038/s42003-020-01160-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1130096533

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/32796916


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317 grid-institutes:grid.69566.3a schema:alternateName Laboratory of Molecular and Cellular Biochemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, 980-8578, Miyagi, Japan
318 schema:name Laboratory of Molecular and Cellular Biochemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, 980-8578, Miyagi, Japan
319 rdf:type schema:Organization
320 grid-institutes:grid.7597.c schema:alternateName Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, 1-7-22 Suehiro-cho, 230-0045, Tsurumi-ku, Yokohama, Japan
321 RIKEN Cluster for Science, Technology and Innovation Hub, 1-7-22 Suehiro-cho, 230-0045, Tsurumi-ku, Yokohama, Japan
322 schema:name Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, 1-7-22 Suehiro-cho, 230-0045, Tsurumi-ku, Yokohama, Japan
323 RIKEN Cluster for Science, Technology and Innovation Hub, 1-7-22 Suehiro-cho, 230-0045, Tsurumi-ku, Yokohama, Japan
324 RIKEN Structural Biology Laboratory, 1-7-22 Suehiro-cho, 230-0045, Tsurumi-ku, Yokohama, Japan
325 rdf:type schema:Organization
 




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