Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds

Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds

Brain-specific angiogenesis inhibitor (BAI) is an adhesion G protein-coupled receptor that acts through the ELMO/DOCK/Rac signaling pathway. Here the authors provide molecular insights into BAI/ELMO interactions by solving the crystal structure of the C-terminal cytoplasmic tail of BAI bound to the...

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Autores principales: Zhuangfeng Weng, Chenghao Situ, Lin Lin, Zhenguo Wu, Jinwei Zhu, Rongguang Zhang
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2019
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Acceso en línea:https://doaj.org/article/d7d9eb07ed314981bfbe7b68e9407b84
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spelling oai:doaj.org-article:d7d9eb07ed314981bfbe7b68e9407b842021-12-02T15:35:40ZStructure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds10.1038/s41467-018-07938-92041-1723https://doaj.org/article/d7d9eb07ed314981bfbe7b68e9407b842019-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07938-9https://doaj.org/toc/2041-1723Brain-specific angiogenesis inhibitor (BAI) is an adhesion G protein-coupled receptor that acts through the ELMO/DOCK/Rac signaling pathway. Here the authors provide molecular insights into BAI/ELMO interactions by solving the crystal structure of the C-terminal cytoplasmic tail of BAI bound to the RAE tandem domains of ELMO2.Zhuangfeng WengChenghao SituLin LinZhenguo WuJinwei ZhuRongguang ZhangNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Zhuangfeng Weng
Chenghao Situ
Lin Lin
Zhenguo Wu
Jinwei Zhu
Rongguang Zhang
Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds
description Brain-specific angiogenesis inhibitor (BAI) is an adhesion G protein-coupled receptor that acts through the ELMO/DOCK/Rac signaling pathway. Here the authors provide molecular insights into BAI/ELMO interactions by solving the crystal structure of the C-terminal cytoplasmic tail of BAI bound to the RAE tandem domains of ELMO2.
format article
author Zhuangfeng Weng
Chenghao Situ
Lin Lin
Zhenguo Wu
Jinwei Zhu
Rongguang Zhang
author_facet Zhuangfeng Weng
Chenghao Situ
Lin Lin
Zhenguo Wu
Jinwei Zhu
Rongguang Zhang
author_sort Zhuangfeng Weng
title Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds
title_short Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds
title_full Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds
title_fullStr Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds
title_full_unstemmed Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds
title_sort structure of bai1/elmo2 complex reveals an action mechanism of adhesion gpcrs via elmo family scaffolds
publisher Nature Portfolio
publishDate 2019
url https://doaj.org/article/d7d9eb07ed314981bfbe7b68e9407b84
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