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Yorodumi- PDB-1d0r: SOLUTION STRUCTURE OF GLUCAGON-LIKE PEPTIDE-1-(7-36)-AMIDE IN TRI... -
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Basic information
| Entry | Database: PDB / ID: 1d0r | ||||||
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| Title | SOLUTION STRUCTURE OF GLUCAGON-LIKE PEPTIDE-1-(7-36)-AMIDE IN TRIFLUOROETHANOL/WATER | ||||||
Components | GLUCAGON-LIKE PEPTIDE-1-(7-36)-AMIDE | ||||||
Keywords | HORMONE/GROWTH FACTOR / SYNTHETIC HORMONE / HORMONE-GROWTH FACTOR COMPLEX | ||||||
| Function / homology | Function and homology informationglucagon receptor binding / : / negative regulation of execution phase of apoptosis / feeding behavior / positive regulation of calcium ion import / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of insulin secretion involved in cellular response to glucose stimulus / positive regulation of gluconeogenesis / cellular response to glucagon stimulus / regulation of insulin secretion ...glucagon receptor binding / : / negative regulation of execution phase of apoptosis / feeding behavior / positive regulation of calcium ion import / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of insulin secretion involved in cellular response to glucose stimulus / positive regulation of gluconeogenesis / cellular response to glucagon stimulus / regulation of insulin secretion / response to activity / gluconeogenesis / hormone activity / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / Glucagon signaling in metabolic regulation / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / Glucagon-type ligand receptors / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / glucose homeostasis / secretory granule lumen / G alpha (s) signalling events / G alpha (q) signalling events / positive regulation of ERK1 and ERK2 cascade / G protein-coupled receptor signaling pathway / receptor ligand activity / endoplasmic reticulum lumen / signaling receptor binding / negative regulation of apoptotic process / extracellular space / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS | ||||||
Authors | Chang, X. / Keller, D. / Bjorn, S. / Led, J.J. | ||||||
Citation | Journal: MAGN.RESON.CHEM. / Year: 2001 Title: Structure and Folding of Glucagon-like Peptide-1-(7-36)-amide in Trifluoroethanol Studied by NMR Authors: Chang, X. / Keller, D. / Bjorn, S. / Led, J.J. #1: Journal: FEBS Lett. / Year: 2002Title: NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer Authors: Chang, X. / Keller, D. / O'Donoghue, S.I. / Led, J.J. | ||||||
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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 | 1d0r.cif.gz | 186.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1d0r.ent.gz | 151.9 KB | Display | PDB format |
| PDBx/mmJSON format | 1d0r.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1d0r_validation.pdf.gz | 352.5 KB | Display | wwPDB validaton report |
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| Full document | 1d0r_full_validation.pdf.gz | 450.2 KB | Display | |
| Data in XML | 1d0r_validation.xml.gz | 15.7 KB | Display | |
| Data in CIF | 1d0r_validation.cif.gz | 24 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d0/1d0r ftp://data.pdbj.org/pub/pdb/validation_reports/d0/1d0r | HTTPS FTP |
-Related structure data
| Similar structure data |
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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: 3302.648 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: RECOMBINANT FORM / Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() |
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-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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| NMR experiment |
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| NMR details | Text: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR TECHNIQUES. |
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Sample preparation
| Details |
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| Sample conditions | pH: 2.5 / Pressure: AMBIENT / Temperature: 300 K | ||||||
| Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
| NMR spectrometer |
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Processing
| NMR software |
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| Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING, RESTRAINED MOLECULAR DYNAMICS Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON 280 NOE-DERIVED DISTANCE CONSTRAINTS, AND 24 DISTANCE RESTRAINTS FROM HYDROGEN BONDS | ||||||||||||
| NMR representative | Selection criteria: lowest energy | ||||||||||||
| NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 40 / Conformers submitted total number: 20 | ||||||||||||
| NMR ensemble rms | Atom type: all backbone atoms / Bond angle rms dev: 3.3 ° / Chain range begin: A / Chain range end: A Coord average rmsd method: THE AVERAGE OF THE RMSD TO THE MEAN OF THE 20 NMR CONFORMERS AS DESCRIBED IN REFERENCE JRNL IS 2.92 ANGSTROMS FOR THE N, C AND CA BACKBONE ATOMS Covalent bond rms dev: 0.0144 Å / Improper torsion angle rms dev: 0.33 ° / Residue range begin: 1 / Residue range end: 30 |
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