6idx
From Proteopedia
Crystal Structure of BAI1/ELMO2 complex
Structural highlights
DiseaseELMO2_HUMAN Ramon syndrome;Primary intraosseous venous malformation. The disease is caused by variants affecting the gene represented in this entry. FunctionELMO2_HUMAN Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Acts in association with DOCK1 and CRK. Was initially proposed to be required in complex with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine nucleotide exchange factor (GEF) activity of DOCK1.[1] [2] [3] [4] Publication Abstract from PubMedThe 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. Structure of BAI1/ELMO2 complex reveals an action mechanism of adhesion GPCRs via ELMO family scaffolds.,Weng Z, Situ C, Lin L, Wu Z, Zhu J, Zhang R Nat Commun. 2019 Jan 3;10(1):51. doi: 10.1038/s41467-018-07938-9. PMID:30604775[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Homo sapiens | Large Structures | Mus musculus | Lin L | Weng ZF | Zhang RG | Zhu JW
