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Yorodumi- PDB-5mgq: Solution structure of oxidized and amidated human IAPP (1-37), th... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5mgq | ||||||||||||
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Title | Solution structure of oxidized and amidated human IAPP (1-37), the diabetes II peptide. | ||||||||||||
Components | Islet amyloid polypeptideAmylin | ||||||||||||
Keywords | PROTEIN FIBRIL / Recombinant human IAPP / Type II Diabetes | ||||||||||||
Function / homology | Function and homology information : / amylin receptor signaling pathway / Calcitonin-like ligand receptors / negative regulation of amyloid fibril formation / negative regulation of bone resorption / eating behavior / negative regulation of osteoclast differentiation / positive regulation of protein kinase A signaling / Regulation of gene expression in beta cells / negative regulation of protein-containing complex assembly ...: / amylin receptor signaling pathway / Calcitonin-like ligand receptors / negative regulation of amyloid fibril formation / negative regulation of bone resorption / eating behavior / negative regulation of osteoclast differentiation / positive regulation of protein kinase A signaling / Regulation of gene expression in beta cells / negative regulation of protein-containing complex assembly / positive regulation of cAMP-mediated signaling / positive regulation of calcium-mediated signaling / bone resorption / sensory perception of pain / osteoclast differentiation / hormone activity / cell-cell signaling / amyloid-beta binding / G alpha (s) signalling events / positive regulation of MAPK cascade / receptor ligand activity / positive regulation of apoptotic process / Amyloid fiber formation / signaling receptor binding / lipid binding / apoptotic process / signal transduction / extracellular space / extracellular region / identical protein binding Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | SOLUTION NMR / molecular dynamics | ||||||||||||
Authors | Rodriguez Camargo, D.C. / Tripsianes, K. / Reif, B. | ||||||||||||
Funding support | Germany, Czech Republic, 3items
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Citation | Journal: Sci Rep / Year: 2017 Title: The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes. Authors: Rodriguez Camargo, D.C. / Tripsianes, K. / Buday, K. / Franko, A. / Gobl, C. / Hartlmuller, C. / Sarkar, R. / Aichler, M. / Mettenleiter, G. / Schulz, M. / Boddrich, A. / Erck, C. / Martens, ...Authors: Rodriguez Camargo, D.C. / Tripsianes, K. / Buday, K. / Franko, A. / Gobl, C. / Hartlmuller, C. / Sarkar, R. / Aichler, M. / Mettenleiter, G. / Schulz, M. / Boddrich, A. / Erck, C. / Martens, H. / Walch, A.K. / Madl, T. / Wanker, E.E. / Conrad, M. / de Angelis, M.H. / Reif, B. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5mgq.cif.gz | 213.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5mgq.ent.gz | 178.8 KB | Display | PDB format |
PDBx/mmJSON format | 5mgq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mg/5mgq ftp://data.pdbj.org/pub/pdb/validation_reports/mg/5mgq | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3908.319 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Residue name "TYC" refers to amidation of C-terminal TYR. Source: (gene. exp.) Homo sapiens (human) / Gene: IAPP Details (production host): Transformed plasmids containing T7 promoter driven expression are repressed until IPTG induction of T7 RNA polymerase from a lac promoter. Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P10997 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Type: solution Contents: 150 uM [U-99% 13C; U-99% 15N] Islet Amyloid Polypeptide (IAPP or Amylin), 90% H2O/10% D2O Label: 15_N13_C hIAPP / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 150 uM / Component: Islet Amyloid Polypeptide (IAPP or Amylin) / Isotopic labeling: [U-99% 13C; U-99% 15N] |
Sample conditions | Details: Lyophilized hIAPP(1-37) was dissolved into NMR buffer (30 mM deuterated acetic acid, pH 5.3) containing 10 % D2O for locking. The samples were measured and stored at 277K. The formation of ...Details: Lyophilized hIAPP(1-37) was dissolved into NMR buffer (30 mM deuterated acetic acid, pH 5.3) containing 10 % D2O for locking. The samples were measured and stored at 277K. The formation of the intramolecular disulfide bond was confirmed by NMR Ionic strength: 0 Not defined / Label: 15_N13_C hIAPP / pH: 5.3 / Pressure: 1 atm / Temperature: 278 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | ||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |