37IC
Doc2b-Munc13 complex with designed binder
Summary for 37IC
| Entry DOI | 10.2210/pdb37ic/pdb |
| EMDB information | 78200 |
| Descriptor | Designed binder,Double C2-like domain-containing protein beta, Unc-13 homolog A (2 entities in total) |
| Functional Keywords | doc2b, munc13, snares, neurotransmitter release, membrane binding, synaptic vesicle fusion, cytosolic protein |
| Biological source | synthetic construct More |
| Total number of polymer chains | 2 |
| Total formula weight | 155456.17 |
| Authors | |
| Primary citation | Rastegar, C.T.,Powell, J.,Wosztyl, A.,David, G.,Jaczynska, K.,Bai, X.C.,Han, Y.,Chen, Z.,Rizo, J. Cryo-EM and NMR Reveal a Membrane-Gated Doc2B-Munc13-1 Complex and a Helical Doc2B-SNARE-Binding Interface. Adv Sci, 2026 Cited by PubMed Abstract: Doc2s modulate neurotransmitter release through interactions with Munc13-1, SNAREs, lipids, and Ca, which involve the Doc2 C domains and Munc13-interacting domain (MID). However, it is unclear how these interactions are coupled, how Doc2s bind to Munc13-1, and how they bind to the SNAREs. Here we determined the cryo-electron microscopy structure of a Doc2B-Munc13-1 complex aided by an AI-designed Munc13-1 binder, revealing how Doc2B MID binds to a Munc13-1 hydrophobic pocket essential for opening syntaxin-1 and explaining why Doc2B inhibits SNARE assembly. NMR and fluorescence spectroscopy show that Doc2B MID binds lipids and that MID-lipid and MID-Munc13-1 interactions are mutually exclusive, suggesting that membrane binding helps release the inhibition of Munc13-1. NMR shows that Doc2B binds to the SNARE complex via two helices of CB. Based on these results and liposome fusion assays, we propose a working model whereby: 1. Doc2B MID-Munc13-1 interactions facilitate synergistic binding of both proteins to the plasma membrane, with the MID inhibiting Munc13-1. 2. Membrane binding facilitates MID-lipid interactions that transiently relieve the inhibition of Munc13-1, allowing SNARE complex assembly. 3. Doc2B binding to the SNARE complex inhibits neurotransmitter release but generates a primed state that mediates neurotransmitter release by an as-yet-unknown mechanism. PubMed: 42973246DOI: 10.1002/advs.78011 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.94 Å) |
Structure validation
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