Abstract:
:Syntaxin 1A plays a central role in neurotransmitter release through multiple protein-protein interactions. We have used NMR spectroscopy to identify an autonomously folded N-terminal domain in syntaxin 1A and to elucidate its three-dimensional structure. This 120-residue N-terminal domain is conserved in plasma membrane syntaxins but not in other syntaxins, indicating a specific role in exocytosis. The domain contains three long alpha helices that form an up-and-down bundle with a left-handed twist. A striking residue conservation is observed throughout a long groove that is likely to provide a specific surface for protein-protein interactions. A highly acidic region binds to the C2A domain of synaptotagmin I in a Ca2+-dependent interaction that may serve as an electrostatic switch in neurotransmitter release.
journal_name
Celljournal_title
Cellauthors
Fernandez I,Ubach J,Dulubova I,Zhang X,Südhof TC,Rizo Jdoi
10.1016/s0092-8674(00)81742-0subject
Has Abstractpub_date
1998-09-18 00:00:00pages
841-9issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(00)81742-0journal_volume
94pub_type
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