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Yorodumi- PDB-1bqt: THREE-DIMENSIONAL STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR-I... -
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-Basic information
Entry | Database: PDB / ID: 1bqt | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR-I (IGF-I) DETERMINED BY 1H-NMR AND DISTANCE GEOMETRY, 6 STRUCTURES | ||||||
Components | INSULIN-LIKE GROWTH FACTOR-I | ||||||
Keywords | GROWTH FACTOR / INSULIN | ||||||
Function / homology | Function and homology information glycolate metabolic process / muscle hypertrophy / negative regulation of oocyte development / positive regulation of trophectodermal cell proliferation / insulin-like growth factor binding protein complex / insulin-like growth factor ternary complex / proteoglycan biosynthetic process / positive regulation of glycoprotein biosynthetic process / myotube cell development / skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration ...glycolate metabolic process / muscle hypertrophy / negative regulation of oocyte development / positive regulation of trophectodermal cell proliferation / insulin-like growth factor binding protein complex / insulin-like growth factor ternary complex / proteoglycan biosynthetic process / positive regulation of glycoprotein biosynthetic process / myotube cell development / skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration / negative regulation of neuroinflammatory response / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / positive regulation of cell growth involved in cardiac muscle cell development / negative regulation of vascular associated smooth muscle cell apoptotic process / bone mineralization involved in bone maturation / IRS-related events triggered by IGF1R / exocytic vesicle / positive regulation of transcription regulatory region DNA binding / cell activation / positive regulation of calcineurin-NFAT signaling cascade / alphav-beta3 integrin-IGF-1-IGF1R complex / positive regulation of Ras protein signal transduction / myoblast differentiation / positive regulation of insulin-like growth factor receptor signaling pathway / myoblast proliferation / muscle organ development / negative regulation of interleukin-1 beta production / positive regulation of DNA binding / positive regulation of cardiac muscle hypertrophy / positive regulation of smooth muscle cell migration / positive regulation of activated T cell proliferation / negative regulation of release of cytochrome c from mitochondria / negative regulation of amyloid-beta formation / negative regulation of smooth muscle cell apoptotic process / negative regulation of tumor necrosis factor production / positive regulation of glycogen biosynthetic process / Synthesis, secretion, and deacylation of Ghrelin / epithelial to mesenchymal transition / SHC-related events triggered by IGF1R / positive regulation of osteoblast differentiation / positive regulation of epithelial cell proliferation / positive regulation of tyrosine phosphorylation of STAT protein / positive regulation of vascular associated smooth muscle cell proliferation / insulin-like growth factor receptor binding / activation of protein kinase B activity / positive regulation of glycolytic process / positive regulation of mitotic nuclear division / positive regulation of smooth muscle cell proliferation / insulin-like growth factor receptor signaling pathway / platelet alpha granule lumen / skeletal system development / negative regulation of extrinsic apoptotic signaling pathway / positive regulation of glucose import / positive regulation of protein secretion / regulation of protein phosphorylation / insulin receptor binding / growth factor activity / wound healing / hormone activity / positive regulation of fibroblast proliferation / integrin binding / cellular response to amyloid-beta / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of peptidyl-tyrosine phosphorylation / Platelet degranulation / regulation of gene expression / response to heat / Ras protein signal transduction / cell population proliferation / positive regulation of ERK1 and ERK2 cascade / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / protein stabilization / positive regulation of cell migration / negative regulation of gene expression / positive regulation of cell population proliferation / positive regulation of gene expression / positive regulation of DNA-templated transcription / negative regulation of apoptotic process / signal transduction / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
Authors | Sato, A. / Nishimura, S. / Ohkubo, T. / Kyogoku, Y. / Koyama, S. / Kobayashi, M. / Yasuda, T. / Kobayashi, Y. | ||||||
Citation | Journal: Int.J.Pept.Protein Res. / Year: 1993 Title: Three-dimensional structure of human insulin-like growth factor-I (IGF-I) determined by 1H-NMR and distance geometry. Authors: Sato, A. / Nishimura, S. / Ohkubo, T. / Kyogoku, Y. / Koyama, S. / Kobayashi, M. / Yasuda, T. / Kobayashi, Y. #1: Journal: J.Biochem.(Tokyo) / Year: 1992 Title: 1H-NMR Assignment and Secondary Structure of Human Insulin-Like Growth Factor-I (Igf-I) in Solution Authors: Sato, A. / Nishimura, S. / Ohkubo, T. / Kyogoku, Y. / Koyama, S. / Kobayashi, M. / Yasuda, T. / Kobayashi, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bqt.cif.gz | 70.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bqt.ent.gz | 57.2 KB | Display | PDB format |
PDBx/mmJSON format | 1bqt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1bqt_validation.pdf.gz | 342.9 KB | Display | wwPDB validaton report |
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Full document | 1bqt_full_validation.pdf.gz | 411.3 KB | Display | |
Data in XML | 1bqt_validation.xml.gz | 15.5 KB | Display | |
Data in CIF | 1bqt_validation.cif.gz | 21.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bq/1bqt ftp://data.pdbj.org/pub/pdb/validation_reports/bq/1bqt | HTTPS FTP |
-Related structure data
Similar structure data |
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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 | Mass: 7663.752 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P05019 |
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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 HOMONUCLEAR NMR SPECTROSCOPY |
-Sample preparation
Details | Contents: H2O/D2O=9/1 CONTAINING 10 ACETIC ACID-D4 |
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Sample conditions | pH: 3 / Pressure: 1 atm / Temperature: 313 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 | ||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 6 |