Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode
Ghrelin is a gastric peptide hormone with important physiological functions, including growth hormone release and appetite-stimulating activity. Here, authors solved the crystal structure of the ghrelin receptor bound to antagonist and suggested a possible mechanism of activation by acyl-modified gh...
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2020-08-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-17554-1 |
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doaj-e7526d5cb5754366b7a2d14fcf34c3e12021-08-22T11:41:10ZengNature Publishing GroupNature Communications2041-17232020-08-011111910.1038/s41467-020-17554-1Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition modeYuki Shiimura0Shoichiro Horita1Akie Hamamoto2Hidetsugu Asada3Kunio Hirata4Misuzu Tanaka5Kenji Mori6Tomoko Uemura7Takuya Kobayashi8So Iwata9Masayasu Kojima10Division of Molecular Genetics, Institute of Life Science, Kurume UniversityDepartment of Cell Biology, Graduate School of Medicine, Kyoto UniversityDivision of Molecular Genetics, Institute of Life Science, Kurume UniversityDepartment of Cell Biology, Graduate School of Medicine, Kyoto UniversityRIKENDivision of Molecular Genetics, Institute of Life Science, Kurume UniversityDepartment of Biochemistry, National Cerebral and Cardiovascular Center Research InstituteDepartment of Cell Biology, Graduate School of Medicine, Kyoto UniversityDepartment of Cell Biology, Graduate School of Medicine, Kyoto UniversityDepartment of Cell Biology, Graduate School of Medicine, Kyoto UniversityDivision of Molecular Genetics, Institute of Life Science, Kurume UniversityGhrelin is a gastric peptide hormone with important physiological functions, including growth hormone release and appetite-stimulating activity. Here, authors solved the crystal structure of the ghrelin receptor bound to antagonist and suggested a possible mechanism of activation by acyl-modified ghrelin.https://doi.org/10.1038/s41467-020-17554-1 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Yuki Shiimura Shoichiro Horita Akie Hamamoto Hidetsugu Asada Kunio Hirata Misuzu Tanaka Kenji Mori Tomoko Uemura Takuya Kobayashi So Iwata Masayasu Kojima |
spellingShingle |
Yuki Shiimura Shoichiro Horita Akie Hamamoto Hidetsugu Asada Kunio Hirata Misuzu Tanaka Kenji Mori Tomoko Uemura Takuya Kobayashi So Iwata Masayasu Kojima Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode Nature Communications |
author_facet |
Yuki Shiimura Shoichiro Horita Akie Hamamoto Hidetsugu Asada Kunio Hirata Misuzu Tanaka Kenji Mori Tomoko Uemura Takuya Kobayashi So Iwata Masayasu Kojima |
author_sort |
Yuki Shiimura |
title |
Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode |
title_short |
Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode |
title_full |
Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode |
title_fullStr |
Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode |
title_full_unstemmed |
Structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode |
title_sort |
structure of an antagonist-bound ghrelin receptor reveals possible ghrelin recognition mode |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2020-08-01 |
description |
Ghrelin is a gastric peptide hormone with important physiological functions, including growth hormone release and appetite-stimulating activity. Here, authors solved the crystal structure of the ghrelin receptor bound to antagonist and suggested a possible mechanism of activation by acyl-modified ghrelin. |
url |
https://doi.org/10.1038/s41467-020-17554-1 |
work_keys_str_mv |
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