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Yorodumi- PDB-1tos: TORPEDO CALIFORNICA ACHR RECEPTOR [ALA76] ANALOGUE COMPLEXED WITH... -
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Basic information
| Entry | Database: PDB / ID: 1tos | ||||||
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| Title | TORPEDO CALIFORNICA ACHR RECEPTOR [ALA76] ANALOGUE COMPLEXED WITH THE ANTI-ACETYLCHOLINE MAB6 MONOCLONAL ANTIBODY | ||||||
Components | ACETYLCHOLINE RECEPTOR [ALA76] MIR ANALOGUE | ||||||
Keywords | TRANSMEMBRANE PROTEIN | ||||||
| Function / homology | Function and homology informationacetylcholine-gated monoatomic cation-selective channel activity / transmembrane signaling receptor activity / postsynaptic membrane Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Orlewski, P. / Tsikaris, V. / Sakarellos, C. / Sakarellos-Daistiotis, M. / Vatzaki, E. / Tzartos, S.J. / Marraud, M. / Cung, M.T. | ||||||
Citation | Journal: Biopolymers / Year: 1996Title: Compared structures of the free nicotinic acetylcholine receptor main immunogenic region (MIR) decapeptide and the antibody-bound [A76]MIR analogue: a molecular dynamics simulation from two-dimensional NMR data. Authors: Orlewski, P. / Marraud, M. / Cung, M.T. / Tsikaris, V. / Sakarellos-Daitsiotis, M. / Sakarellos, C. / Vatzaki, E. / Tzartos, S.J. #1: Journal: Biopolymers / Year: 1993Title: Conformational Requirements for Molecular Recognition of Acetylcholine Receptor Main Immunogenic Region (Mir) Analogues by Monoclonal Anti-Mir Antibody: A Two-Dimensional Nuclear Magnetic ...Title: Conformational Requirements for Molecular Recognition of Acetylcholine Receptor Main Immunogenic Region (Mir) Analogues by Monoclonal Anti-Mir Antibody: A Two-Dimensional Nuclear Magnetic Resonance and Molecular Dynamics Approach Authors: Tsikaris, V. / Desticas, E. / Sakarellos-Daistiotis, M. / Sakarellos, C. / Cung, M.T. / Marraud, M. / Vatzaki, E. / Tzartos, S.J. #2: Journal: Pept.Res. / Year: 1992Title: 2D-NMR and Molecular Dynamics Analysis of the Torpedo Californica Acetylcholine Receptor Alpha67-76 Fragment and of its [Ala76]-Analogue Authors: Cung, M.T. / Tsikaris, V. / Demange, P. / Papadouli, I. / Tzartos, S. / Sakarellos, C. / Marraud, M. #3: Journal: Biopolymers / Year: 1991Title: Two-Dimensional 1H-NMR Study of Antigen-Antibody Interactions: Binding of Synthetic Decapeptides to an Anti-Acetylcholine Receptor Monoclonal Antibody Authors: Cung, M.T. / Demange, P. / Marraud, M. / Tsikaris, V. / Papadouli, I. / Sakarellos, C. / Kokla, A. / Tzartos, S.J. #4: Journal: Biopolymers / Year: 1989Title: Two-Dimensional 1H-NMR Study of Synthetic Peptides Containing the Main Immunogenic Region of the Torpedo Acetylcholine Receptor Authors: Cung, M.T. / Marraud, M. / Hadjidakis, I. / Bairaktari, E. / Sakarellos, C. / Kokla, A. / J Tzartos, S. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1tos.cif.gz | 14 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1tos.ent.gz | 8.7 KB | Display | PDB format |
| PDBx/mmJSON format | 1tos.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1tos_validation.pdf.gz | 340.5 KB | Display | wwPDB validaton report |
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| Full document | 1tos_full_validation.pdf.gz | 347.9 KB | Display | |
| Data in XML | 1tos_validation.xml.gz | 2.2 KB | Display | |
| Data in CIF | 1tos_validation.cif.gz | 2.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/to/1tos ftp://data.pdbj.org/pub/pdb/validation_reports/to/1tos | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1torC C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 1063.121 Da / Num. of mol.: 1 / Fragment: ALPHA 67-76 DOMAIN OF THE ACETYLCHOLINE RECEPTOR / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P02710 |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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Sample preparation
| Crystal grow | *PLUS Method: other |
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Processing
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| NMR ensemble | Conformers submitted total number: 3 |
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