6IDX
Crystal Structure of BAI1/ELMO2 complex
Summary for 6IDX
| Entry DOI | 10.2210/pdb6idx/pdb |
| Descriptor | Engulfment and cell motility protein 2, Adhesion G protein-coupled receptor B1 (3 entities in total) |
| Functional Keywords | adhesion gpcrs, cell adhesion |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 63064.36 |
| Authors | Weng, Z.F.,Lin, L.,Zhu, J.W.,Zhang, R.G. (deposition date: 2018-09-11, release date: 2019-01-23, Last modification date: 2023-11-22) |
| Primary citation | 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 Cited by 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: 30604775DOI: 10.1038/s41467-018-07938-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.699 Å) |
Structure validation
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