Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A.
Cell
; 94(6): 841-9, 1998 Sep 18.
Article
en En
| MEDLINE
| ID: mdl-9753330
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.
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Bases de datos:
MEDLINE
Asunto principal:
Evolución Molecular
/
Antígenos de Superficie
/
Proteínas del Tejido Nervioso
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Cell
Año:
1998
Tipo del documento:
Article
País de afiliación:
Estados Unidos