Structure of the complex of C1q-like 3 protein with adhesion-GPCR BAI3 DOI Creative Commons
Yi Miao, Haoqing Wang, Kevin M. Jude

et al.

Communications Biology, Journal Year: 2025, Volume and Issue: 8(1)

Published: May 3, 2025

Abstract The adhesion-GPCR Brain-specific Angiogenesis Inhibitor-3 (BAI3) plays a crucial role in organizing synapses the brain. However, how BAI3 engages one of its ligands, C1q-like proteins (C1qls), remains largely unexplored. Here, we present single-particle cryo-electron microscopy (cryo-EM) structure C1ql3-BAI3 complex at 2.8 Å resolution. reveals hexameric configuration, where C1ql3 forms central homotrimer that effectively captures three molecules. These molecules fit snugly into grooves between trimeric C1q domains C1qls, employing calcium ion (Ca 2+ )-mediated interactions differ from previously characterized structures domain-mediated complexes. Furthermore, conducted mutant analysis and cell surface staining, which confirmed essential contact residues involved this interaction. This unique binding mechanism not only enhances our understanding C1ql-BAI3-mediated synaptic organization but also sheds light on functional dynamics

Language: Английский

Structure of the complex of C1q-like 3 protein with adhesion-GPCR BAI3 DOI Creative Commons
Yi Miao, Haoqing Wang, Kevin M. Jude

et al.

Communications Biology, Journal Year: 2025, Volume and Issue: 8(1)

Published: May 3, 2025

Abstract The adhesion-GPCR Brain-specific Angiogenesis Inhibitor-3 (BAI3) plays a crucial role in organizing synapses the brain. However, how BAI3 engages one of its ligands, C1q-like proteins (C1qls), remains largely unexplored. Here, we present single-particle cryo-electron microscopy (cryo-EM) structure C1ql3-BAI3 complex at 2.8 Å resolution. reveals hexameric configuration, where C1ql3 forms central homotrimer that effectively captures three molecules. These molecules fit snugly into grooves between trimeric C1q domains C1qls, employing calcium ion (Ca 2+ )-mediated interactions differ from previously characterized structures domain-mediated complexes. Furthermore, conducted mutant analysis and cell surface staining, which confirmed essential contact residues involved this interaction. This unique binding mechanism not only enhances our understanding C1ql-BAI3-mediated synaptic organization but also sheds light on functional dynamics

Language: Английский

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