1BR0

THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A

1BR0 の概要

• エントリーDOI: 10.2210/pdb1br0/pdb
• NMR情報: BMRB: 4198
• 分子名称: PROTEIN (SYNTAXIN 1-A) (1 entity in total)
• 機能のキーワード: syntaxin, membrane fusion, synaptic vesicle exocytosis, membrane protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein (By similarity): P32851
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14135.80

構造登録者

Fernandez, I.,Ubach, J.,Dubulova, I.,Zhang, X.,Sudhof, T.C.,Rizo, J. (登録日: 1998-08-25, 公開日: 1998-09-02, 最終更新日: 2024-05-22)

主引用文献

Fernandez, I.,Ubach, J.,Dulubova, I.,Zhang, X.,Sudhof, T.C.,Rizo, J.
Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A.
Cell(Cambridge,Mass.), 94:841-849, 1998

PubMed 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.

PubMed: 9753330
DOI: 10.1016/S0092-8674(00)81742-0

実験手法

SOLUTION NMR