6IDX

Crystal Structure of BAI1/ELMO2 complex

6IDX の概要

• エントリーDOI: 10.2210/pdb6idx/pdb
• 分子名称: Engulfment and cell motility protein 2, Adhesion G protein-coupled receptor B1 (3 entities in total)
• 機能のキーワード: adhesion gpcrs, cell adhesion
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 63064.36

構造登録者

Weng, Z.F.,Lin, L.,Zhu, J.W.,Zhang, R.G. (登録日: 2018-09-11, 公開日: 2019-01-23, 最終更新日: 2023-11-22)

主引用文献

Weng, Z.,Situ, C.,Lin, L.,Wu, Z.,Zhu, J.,Zhang, R.
Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds
Nat Commun, 10:51-51, 2019

PubMed Abstract: The brain-specific angiogenesis inhibitor (BAI) subfamily of adhesion G protein-coupled receptors (aGPCRs) plays crucial roles in diverse cellular processes including phagocytosis, myoblast fusion, and synaptic development through the ELMO/DOCK/Rac signaling pathway, although the underlying molecular mechanism is not well understood. Here, we demonstrate that an evolutionarily conserved fragment located in the C-terminal cytoplasmic tail of BAI-aGPCRs is specifically recognized by the RBD-ARR-ELMO (RAE) supramodule of the ELMO family scaffolds. The crystal structures of ELMO2-RAE and its complex with BAI1 uncover the molecular basis of BAI/ELMO interactions. Based on the complex structure we identify aGPCR-GPR128 as another upstream receptor for the ELMO family scaffolds, most likely with a recognition mode similar to that of BAI/ELMO interactions. Finally, we map disease-causing mutations of BAI and ELMO and analyze their effects on complex formation.

PubMed: 30604775
DOI: 10.1038/s41467-018-07938-9

実験手法

X-RAY DIFFRACTION (1.699 Å)