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- PDB-1igl: SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR II RELATIO... -
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Basic information
Entry | Database: PDB / ID: 1igl | ||||||
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Title | SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR II RELATIONSHIP TO RECEPTOR AND BINDING PROTEIN INTERACTIONS | ||||||
![]() | INSULIN-LIKE GROWTH FACTOR II | ||||||
![]() | GROWTH FACTOR | ||||||
Function / homology | ![]() spongiotrophoblast cell proliferation / negative regulation of muscle cell differentiation / positive regulation of skeletal muscle tissue growth / embryonic placenta morphogenesis / regulation of muscle cell differentiation / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / IRS-related events triggered by IGF1R / genomic imprinting / positive regulation of organ growth / exocrine pancreas development ...spongiotrophoblast cell proliferation / negative regulation of muscle cell differentiation / positive regulation of skeletal muscle tissue growth / embryonic placenta morphogenesis / regulation of muscle cell differentiation / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / IRS-related events triggered by IGF1R / genomic imprinting / positive regulation of organ growth / exocrine pancreas development / positive regulation of multicellular organism growth / positive regulation of vascular endothelial cell proliferation / transmembrane receptor protein tyrosine kinase activator activity / positive regulation of activated T cell proliferation / positive regulation of cell division / positive regulation of glycogen biosynthetic process / embryonic placenta development / SHC-related events triggered by IGF1R / positive regulation of insulin receptor signaling pathway / striated muscle cell differentiation / insulin-like growth factor receptor binding / positive regulation of mitotic nuclear division / protein serine/threonine kinase activator activity / insulin-like growth factor receptor signaling pathway / platelet alpha granule lumen / animal organ morphogenesis / insulin receptor binding / growth factor activity / hormone activity / osteoblast differentiation / glucose metabolic process / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / integrin binding / Platelet degranulation / insulin receptor signaling pathway / in utero embryonic development / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor ligand activity / positive regulation of cell population proliferation / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Torres, A.M. / Forbes, B.E. / Aplin, S.E. / Wallace, J.C. / Francis, G.L. / Norton, R.S. | ||||||
![]() | ![]() Title: Solution structure of human insulin-like growth factor II. Relationship to receptor and binding protein interactions. Authors: Torres, A.M. / Forbes, B.E. / Aplin, S.E. / Wallace, J.C. / Francis, G.L. / Norton, R.S. #1: ![]() Title: Insulin-Like Growth Factors I and II Authors: Humbel, R.E. #2: ![]() Title: Tertiary Structures, Receptor Binding, and Antigenicity of Insulinlike Growth Factors Authors: Blundell, T.L. / Bedarkar, S. / Humbel, R.E. #3: ![]() Title: Insulin-Like Growth Factor: A Model for Tertiary Structure Accounting for Immmunoreactivity and Receptor Binding Authors: Blundell, T.L. / Bedarkar, S. / Rinderknecht, E. / Humbel, R.E. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 398 KB | Display | ![]() |
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PDB format | ![]() | 342.9 KB | Display | ![]() |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Atom site foot note | 1: ARG 30 - PRO 31 MODEL 5 OMEGA = 213.63 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: ARG 3 - PRO 4 MODEL 13 OMEGA = 148.68 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: THR 62 - PRO 63 MODEL 18 OMEGA = 148.91 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | |||||||||
NMR ensembles |
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Components
#1: Protein | Mass: 7484.472 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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-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 | Name: ![]() | ||||||||
NMR ensemble | Conformers submitted total number: 20 |