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- PDB-1t1k: NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS-B10-ASP, VAL-B12-ALA, P... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1t1k | ||||||
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Title | NMR STRUCTURE OF HUMAN INSULIN MUTANT HIS-B10-ASP, VAL-B12-ALA, PRO-B28-LYS, LYS-B29-PRO, 15 STRUCTURES | ||||||
![]() | (Insulin) x 2 | ||||||
![]() | HORMONE/GROWTH FACTOR / Ala-B12-DKP-insulin / protein unfolding / insulin receptor / receptor binding / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | ![]() negative regulation of NAD(P)H oxidase activity / negative regulation of glycogen catabolic process / regulation of cellular amino acid metabolic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / Signaling by Insulin receptor / IRS activation / Insulin processing / 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 / positive regulation of nitric oxide mediated signal transduction / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / Signaling by Insulin receptor / IRS activation / Insulin processing / regulation of protein secretion / positive regulation of respiratory burst / positive regulation of peptide hormone secretion / Regulation of gene expression in beta cells / negative regulation of acute inflammatory response / alpha-beta T cell activation / negative regulation of respiratory burst involved in inflammatory response / positive regulation of dendritic spine maintenance / positive regulation of glycogen biosynthetic process / Synthesis, secretion, and deacylation of Ghrelin / negative regulation of protein secretion / regulation of protein localization to plasma membrane / fatty acid homeostasis / Signal attenuation / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / negative regulation of lipid catabolic process / negative regulation of gluconeogenesis / COPI-mediated anterograde transport / positive regulation of lipid biosynthetic process / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / negative regulation of reactive oxygen species biosynthetic process / positive regulation of insulin receptor signaling pathway / nitric oxide-cGMP-mediated signaling / transport vesicle / positive regulation of protein autophosphorylation / Insulin receptor recycling / neuron projection maintenance / NPAS4 regulates expression of target genes / positive regulation of protein metabolic process / positive regulation of brown fat cell differentiation / positive regulation of glycolytic process / activation of protein kinase B activity / endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of mitotic nuclear division / Insulin receptor signalling cascade / positive regulation of nitric-oxide synthase activity / positive regulation of cytokine production / positive regulation of long-term synaptic potentiation / Regulation of insulin secretion / acute-phase response / endosome lumen / positive regulation of protein secretion / positive regulation of glucose import / positive regulation of cell differentiation / negative regulation of proteolysis / regulation of transmembrane transporter activity / insulin-like growth factor receptor binding / wound healing / insulin receptor binding / regulation of synaptic plasticity / negative regulation of protein catabolic process / hormone activity / cognition / positive regulation of neuron projection development / positive regulation of protein localization to nucleus / Golgi lumen / vasodilation / glucose metabolic process / regulation of protein localization / insulin receptor signaling pathway / cell-cell signaling / glucose homeostasis / 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 | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING | ||||||
![]() | Huang, K. / Xu, B. / Hu, S.Q. / Chu, Y.C. / Hua, Q.X. / Whittaker, J. / Nakagawa, S.H. / De Meyts, P. / Katsoyannis, P.G. / Weiss, M.A. | ||||||
![]() | ![]() Title: How Insulin Binds: the B-Chain alpha-Helix Contacts the L1 beta-Helix of the Insulin Receptor. Authors: Huang, K. / Xu, B. / Hu, S.Q. / Chu, Y.C. / Hua, Q.X. / Qu, Y. / Li, B. / Wang, S. / Wang, R.Y. / Nakagawa, S.H. / Theede, A.M. / Whittaker, J. / De Meyts, P. / Katsoyannis, P.G. / Weiss, M.A. #1: Journal: Biochemistry / Year: 2000 Title: MUTATIONAL ANALYSIS OF INVARIANT VALINE B12 IN INSULIN: IMPLICATION FOR RECEPTOR BINDING Authors: Nakagawa, S.H. / Tager, H.S. / Steiner, D.F. #2: ![]() Title: ALANINE SCANNING MUTAGENESIS OF INSULIN Authors: Kristen, C. / Kjeldsen, T. / Wiberg, F.C. / Schaffer, L. / Hach, M. / Havelund, S. / Bass, J. / Steiner, D.F. / Andersen, A.S. #3: Journal: BIOCHEM.MOL.BIOL.INT. / Year: 1996 Title: STUDIES ON RECEPTOR BINDING SITE OF INSULIN: THE HYDROPHOBIC B12VAL CAN BE SUBSTITUTED BY HYDROPHILIC THR Authors: Wang, Q.Q. / Feng, Y.M. / Zhang, Y.S. #4: Journal: Biochemistry / Year: 1993 Title: STERIC REQUIRMENTS AT POSITION B12 FOR HIGH BIOLOGICAL ACTIVITY IN INSULIN Authors: Hu, S.Q. / Burke, G.T. / Schwartz, G.P. / Ferderigos, N. / Ross, J.B. / Katsoyannis, P.G. #5: Journal: INT.J.PEPT.PROTEIN RES. / Year: 1981 Title: [12-ASPARAGINE-B] HUMAN INSULIN. AN ANALOGUE WITH MODIFICATION IN THE HYDROPHOBIC CORE OF INSULIN Authors: Schwartz, G.P. / Burke, P.G. / Katsoyannis, P.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 227.9 KB | Display | ![]() |
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PDB format | ![]() | 197.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 356.1 KB | Display | ![]() |
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Full document | ![]() | 536.6 KB | Display | |
Data in XML | ![]() | 20.7 KB | Display | |
Data in CIF | ![]() | 31.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 2383.698 Da / Num. of mol.: 1 / Fragment: INSULIN A CHAIN Mutation: HIS-B10-ASP, VAL-B12-ALA, PRO-B28-LYS, LYS-B29-PRO Source method: obtained synthetically Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS(HUMAN) References: UniProt: P01308 |
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#2: Protein/peptide | Mass: 3382.841 Da / Num. of mol.: 1 / Fragment: INSULIN B CHAIN / Source method: obtained synthetically Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OF THE PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS(HUMAN) References: UniProt: P01308 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined by using standard 2D homonuclear techniques |
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Sample preparation
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1 Details: the structures are based on a total of 668 restraints: 607 are NOE-derived distance constraints, 39 are dihedral angle restraints, 22 are hydrogen bond restraints. | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 15 |