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Yorodumi- PDB-1mhi: THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN INSULIN DIMER. A STUDY... -
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-Basic information
Entry | Database: PDB / ID: 1mhi | ||||||
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Title | THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN INSULIN DIMER. A STUDY OF THE B9(ASP) MUTANT OF HUMAN INSULIN USING NUCLEAR MAGNETIC RESONANCE DISTANCE GEOMETRY AND RESTRAINED MOLECULAR DYNAMICS | ||||||
Components | (INSULIN) x 2 | ||||||
Keywords | HORMONE | ||||||
Function / homology | Function and homology information negative regulation of NAD(P)H oxidase activity / negative regulation of glycogen catabolic process / regulation of cellular amino acid metabolic process / Signaling by Insulin receptor / IRS activation / nitric oxide-cGMP-mediated signaling / negative regulation of fatty acid metabolic process / Insulin processing / negative regulation of feeding behavior / regulation of protein secretion ...negative regulation of NAD(P)H oxidase activity / negative regulation of glycogen catabolic process / regulation of cellular amino acid metabolic process / Signaling by Insulin receptor / IRS activation / nitric oxide-cGMP-mediated signaling / negative regulation of fatty acid metabolic process / Insulin processing / negative regulation of feeding behavior / regulation of protein secretion / positive regulation of peptide hormone secretion / Regulation of gene expression in beta cells / positive regulation of respiratory burst / positive regulation of dendritic spine maintenance / alpha-beta T cell activation / negative regulation of acute inflammatory response / negative regulation of respiratory burst involved in inflammatory response / negative regulation of protein secretion / fatty acid homeostasis / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of glycogen biosynthetic process / positive regulation of lipid biosynthetic process / Signal attenuation / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / negative regulation of gluconeogenesis / positive regulation of nitric oxide mediated signal transduction / regulation of protein localization to plasma membrane / COPI-mediated anterograde transport / negative regulation of lipid catabolic process / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / positive regulation of insulin receptor signaling pathway / negative regulation of reactive oxygen species biosynthetic process / transport vesicle / positive regulation of protein autophosphorylation / Insulin receptor recycling / insulin-like growth factor receptor binding / NPAS4 regulates expression of target genes / positive regulation of protein metabolic process / neuron projection maintenance / endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of brown fat cell differentiation / activation of protein kinase B activity / positive regulation of glycolytic process / Insulin receptor signalling cascade / positive regulation of mitotic nuclear division / Regulation of insulin secretion / positive regulation of nitric-oxide synthase activity / positive regulation of long-term synaptic potentiation / endosome lumen / positive regulation of cytokine production / acute-phase response / positive regulation of protein secretion / regulation of transmembrane transporter activity / positive regulation of cell differentiation / positive regulation of glucose import / negative regulation of proteolysis / regulation of synaptic plasticity / wound healing / insulin receptor binding / negative regulation of protein catabolic process / positive regulation of neuron projection development / hormone activity / cognition / Golgi lumen / vasodilation / positive regulation of protein localization to nucleus / glucose metabolic process / regulation of protein localization / glucose homeostasis / cell-cell signaling / insulin receptor signaling pathway / positive regulation of NF-kappaB transcription factor activity / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of cell growth / secretory granule lumen / protease binding / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of cell migration / G protein-coupled receptor signaling pathway / Amyloid fiber formation / endoplasmic reticulum lumen / Golgi membrane / negative regulation of gene expression / positive regulation of cell population proliferation / positive regulation of gene expression / regulation of DNA-templated transcription / extracellular space / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Jorgensen, A.M.M. / Kristensen, S.M. / Led, J.J. / Balschmidt, P. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1992 Title: Three-dimensional solution structure of an insulin dimer. A study of the B9(Asp) mutant of human insulin using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. Authors: Jorgensen, A.M. / Kristensen, S.M. / Led, J.J. / Balschmidt, P. #1: Journal: Magn.Reson.Chem. / Year: 1995 Title: A Carbon-13 NMR Study of the B9(Asp) Mutant of Human Insulin Authors: Kristensen, S.M. / Led, J.J. #2: Journal: Biochemistry / Year: 1994 Title: Structural Details of Asp(B9) Human Insulin at Low Ph from 2D NMR Titration Studies Authors: Sorensen, M.D. / Led, J.J. #3: Journal: J.Am.Chem.Soc. / Year: 1994 Title: A New Linear Prediction Model Method for the Determination of Slow Amide Proton Exchange Rates from a Series of One-Dimensional 1H NMR Spectra Authors: Moss, R. / Gesmar, H. / Led, J.J. #4: Journal: J.Am.Chem.Soc. / Year: 1993 Title: Slow Amide Proton Exchange Rates from the Line Widths in a Single Two-Dimensional 1H NMR Spectrum Authors: Olsen, H.B. / Gesmar, H. / Led, J.J. #5: Journal: J.Mol.Biol. / Year: 1991 Title: Proton Nuclear Magnetic Resonance Study of the B9(Asp) Mutant of Human Insulin. Sequential Assignment and Secondary Structure Authors: Kristensen, S.M. / Jorgensen, A.M.M. / Led, J.J. / Balschmidt, P. / Hansen, F.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mhi.cif.gz | 343.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mhi.ent.gz | 298.3 KB | Display | PDB format |
PDBx/mmJSON format | 1mhi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mh/1mhi ftp://data.pdbj.org/pub/pdb/validation_reports/mh/1mhi | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Atom site foot note | 1: THR B 27 - PRO B 28 MODEL 1 OMEGA = 41.00 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: THR B 27 - PRO B 28 MODEL 3 OMEGA = 214.06 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: THR B 27 - PRO B 28 MODEL 4 OMEGA = 213.37 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: THR B 27 - PRO B 28 MODEL 8 OMEGA = 216.24 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: THR B 27 - PRO B 28 MODEL 10 OMEGA = 241.03 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 6: THR B 27 - PRO B 28 MODEL 11 OMEGA = 217.65 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 7: THR B 27 - PRO B 28 MODEL 13 OMEGA = 233.42 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 8: CIS PROLINE - PRO B 28 MODEL 15 9: THR B 27 - PRO B 28 MODEL 19 OMEGA = 240.85 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 10: THR B 27 - PRO B 28 MODEL 20 OMEGA = 91.63 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | |||||||||
NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2383.698 Da / Num. of mol.: 1 / Mutation: S(B 9)D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P01308 |
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#2: Protein/peptide | Mass: 3461.963 Da / Num. of mol.: 1 / Mutation: S(B 9)D Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P01308 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
NMR software |
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NMR ensemble | Conformers submitted total number: 20 |