7r85 | pdb_00007r85
Structure of mouse Bai1 (ADGRB1) TSR3 domain
Structural highlights
Function[AGRB1_MOUSE] Phosphatidylserine receptor which enhances the engulfment of apoptotic cells (PubMed:17960134). Also mediates the binding and engulfment of Gram-negative bacteria (PubMed:21245295, PubMed:26838550, PubMed:26838550). Stimulates production of reactive oxygen species by macrophages in response to Gram-negative bacteria, resulting in enhanced microbicidal macrophage activity (By similarity). In the gastric mucosa, required for recognition and engulfment of apoptotic gastric epithelial cells (By similarity). Promotes myoblast fusion (PubMed:23615608). Activates the Rho pathway in a G-protein-dependent manner (By similarity). Inhibits MDM2-mediated ubiquitination and degradation of DLG4/PSD95, promoting DLG4 stability and regulating synaptic plasticity (PubMed:25751059). Required for the formation of dendritic spines by ensuring the correct localization of PARD3 and TIAM1 (By similarity). Potent inhibitor of angiogenesis in brain and may play a significant role as a mediator of the p53/TP53 signal in suppression of glioblastoma (By similarity).[UniProtKB:C0HL12][UniProtKB:O14514][1] [2] [3] [4] [5] [6] Inhibits angiogenesis in a CD36-dependent manner.[UniProtKB:O14514] Inhibits angiogenesis.[UniProtKB:O14514] Publication Abstract from PubMedRTN4-binding proteins were widely studied as "NoGo" receptors, but their physiological interactors and roles remain elusive. Similarly, BAI adhesion-GPCRs were associated with numerous activities, but their ligands and functions remain unclear. Using unbiased approaches, we observed an unexpected convergence: RTN4 receptors are high-affinity ligands for BAI adhesion-GPCRs. A single thrombospondin type 1-repeat (TSR) domain of BAIs binds to the leucine-rich repeat domain of all three RTN4-receptor isoforms with nanomolar affinity. In the 1.65 A crystal structure of the BAI1/RTN4-receptor complex, C-mannosylation of tryptophan and O-fucosylation of threonine in the BAI TSR-domains creates a RTN4-receptor/BAI interface shaped by unusual glycoconjugates that enables high-affinity interactions. In human neurons, RTN4 receptors regulate dendritic arborization, axonal elongation, and synapse formation by differential binding to glial versus neuronal BAIs, thereby controlling neural network activity. Thus, BAI binding to RTN4/NoGo receptors represents a receptor-ligand axis that, enabled by rare post-translational modifications, controls development of synaptic circuits. RTN4/NoGo-receptor binding to BAI adhesion-GPCRs regulates neuronal development.,Wang J, Miao Y, Wicklein R, Sun Z, Wang J, Jude KM, Fernandes RA, Merrill SA, Wernig M, Garcia KC, Sudhof TC Cell. 2021 Nov 24;184(24):5869-5885.e25. doi: 10.1016/j.cell.2021.10.016. Epub, 2021 Nov 9. PMID:34758294[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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