1BR0
THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A
Summary for 1BR0
| Entry DOI | 10.2210/pdb1br0/pdb |
| NMR Information | BMRB: 4198 |
| Descriptor | PROTEIN (SYNTAXIN 1-A) (1 entity in total) |
| Functional Keywords | syntaxin, membrane fusion, synaptic vesicle exocytosis, membrane protein |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein (By similarity): P32851 |
| Total number of polymer chains | 1 |
| Total formula weight | 14135.80 |
| Authors | Fernandez, I.,Ubach, J.,Dubulova, I.,Zhang, X.,Sudhof, T.C.,Rizo, J. (deposition date: 1998-08-25, release date: 1998-09-02, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 9753330DOI: 10.1016/S0092-8674(00)81742-0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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