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Yorodumi- PDB-1hit: Receptor binding redefined by a structural switch in a mutant Hum... -
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Basic information
| Entry | Database: PDB / ID: 1hit | ||||||
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| Title | Receptor binding redefined by a structural switch in a mutant Human Insulin | ||||||
Components | (INSULIN) x 2 | ||||||
Keywords | HORMONE | ||||||
| Function / homology | Function and homology informationnegative regulation of glycogen catabolic 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 / regulation of protein secretion / Insulin processing / positive regulation of peptide hormone secretion / positive regulation of respiratory burst ...negative regulation of glycogen catabolic 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 / regulation of protein secretion / Insulin processing / positive regulation of peptide hormone secretion / positive regulation of respiratory burst / negative regulation of acute inflammatory response / Regulation of gene expression in beta cells / alpha-beta T cell activation / positive regulation of dendritic spine maintenance / Synthesis, secretion, and deacylation of Ghrelin / negative regulation of respiratory burst involved in inflammatory response / activation of protein kinase B activity / negative regulation of protein secretion / negative regulation of gluconeogenesis / positive regulation of insulin receptor signaling pathway / positive regulation of glycogen biosynthetic process / fatty acid homeostasis / Signal attenuation / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / negative regulation of lipid catabolic process / positive regulation of lipid biosynthetic process / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / regulation of protein localization to plasma membrane / nitric oxide-cGMP-mediated signaling / transport vesicle / COPI-mediated anterograde transport / positive regulation of nitric-oxide synthase activity / Insulin receptor recycling / negative regulation of reactive oxygen species biosynthetic process / insulin-like growth factor receptor binding / positive regulation of brown fat cell differentiation / NPAS4 regulates expression of target genes / neuron projection maintenance / endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of mitotic nuclear division / Insulin receptor signalling cascade / positive regulation of cytokine production / positive regulation of glycolytic process / endosome lumen / positive regulation of long-term synaptic potentiation / acute-phase response / positive regulation of protein secretion / positive regulation of D-glucose import / insulin receptor binding / Regulation of insulin secretion / positive regulation of cell differentiation / wound healing / positive regulation of neuron projection development / hormone activity / negative regulation of protein catabolic process / regulation of synaptic plasticity / positive regulation of protein localization to nucleus / Golgi lumen / vasodilation / cognition / glucose metabolic process / insulin receptor signaling pathway / glucose homeostasis / cell-cell signaling / regulation of protein localization / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of cell growth / protease binding / secretory granule lumen / positive regulation of canonical NF-kappaB signal transduction / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of MAPK cascade / positive regulation of cell migration / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / Amyloid fiber formation / 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 | Hua, Q.X. / Kochoyan, M. / Weiss, M.A. | ||||||
Citation | Journal: Nature / Year: 1991Title: Receptor binding redefined by a structural switch in a mutant human insulin. Authors: Hua, Q.X. / Shoelson, S.E. / Kochoyan, M. / Weiss, M.A. | ||||||
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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 | 1hit.cif.gz | 142 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1hit.ent.gz | 115.7 KB | Display | PDB format |
| PDBx/mmJSON format | 1hit.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1hit_validation.pdf.gz | 360.6 KB | Display | wwPDB validaton report |
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| Full document | 1hit_full_validation.pdf.gz | 456 KB | Display | |
| Data in XML | 1hit_validation.xml.gz | 10.3 KB | Display | |
| Data in CIF | 1hit_validation.cif.gz | 16.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hi/1hit ftp://data.pdbj.org/pub/pdb/validation_reports/hi/1hit | HTTPS FTP |
-Related structure data
| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Atom site foot note | 1: THR B 27 - PRO B 28 MODEL 5 OMEGA =220.40 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: THR B 27 - PRO B 28 MODEL 7 OMEGA =134.22 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: THR B 27 - PRO B 28 MODEL 8 OMEGA =131.54 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 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P01308 |
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| #2: Protein/peptide | Mass: 3343.831 Da / Num. of mol.: 1 / Mutation: F24G Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P01308 |
| Has protein modification | Y |
-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
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| NMR software |
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| NMR ensemble | Conformers submitted total number: 9 |
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Homo sapiens (human)
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