Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A.

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

Cell

journal_title

Cell

authors

Fernandez I,Ubach J,Dulubova I,Zhang X,Südhof TC,Rizo J

doi

10.1016/s0092-8674(00)81742-0

subject

Has Abstract

pub_date

1998-09-18 00:00:00

pages

841-9

issue

6

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(00)81742-0

journal_volume

94

pub_type

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