3MPP
Botulinum Neurotoxin Type G Receptor Binding Domain
Summary for 3MPP
Entry DOI | 10.2210/pdb3mpp/pdb |
Descriptor | Botulinum neurotoxin type G (2 entities in total) |
Functional Keywords | beta barrel beta trefoil, toxin |
Biological source | Clostridium botulinum |
Cellular location | Secreted (By similarity): Q60393 |
Total number of polymer chains | 1 |
Total formula weight | 50678.64 |
Authors | Schmitt, J.M.,Lacy, D.B. (deposition date: 2010-04-27, release date: 2010-06-16, Last modification date: 2023-09-06) |
Primary citation | Schmitt, J.,Karalewitz, A.,Benefield, D.A.,Mushrush, D.J.,Pruitt, R.N.,Spiller, B.W.,Barbieri, J.T.,Lacy, D.B. Structural analysis of botulinum neurotoxin type G receptor binding . Biochemistry, 49:5200-5205, 2010 Cited by PubMed Abstract: Botulinum neurotoxin (BoNT) binds peripheral neurons at the neuromuscular junction through a dual-receptor mechanism that includes interactions with ganglioside and protein receptors. The receptor identities vary depending on BoNT serotype (A-G). BoNT/B and BoNT/G bind the luminal domains of synaptotagmin I and II, homologous synaptic vesicle proteins. We observe conditions under which BoNT/B binds both Syt isoforms, but BoNT/G binds only SytI. Both serotypes bind ganglioside G(T1b). The BoNT/G receptor-binding domain crystal structure provides a context for examining these binding interactions and a platform for understanding the physiological relevance of different Syt receptor isoforms in vivo. PubMed: 20507178DOI: 10.1021/bi100412v PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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