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- PDB-2gf1: SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR 1: A NUCLE... -

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Basic information

Entry
Database: PDB / ID: 2gf1
TitleSOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR 1: A NUCLEAR MAGNETIC RESONANCE AND RESTRAINED MOLECULAR DYNAMICS STUDY
ComponentsINSULIN-LIKE GROWTH FACTOR IInsulin-like growth factor 1
KeywordsGROWTH FACTOR
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 / positive regulation of cell growth involved in cardiac muscle cell development / negative regulation of vascular associated smooth muscle cell apoptotic process / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / bone mineralization involved in bone maturation / IRS-related events triggered by IGF1R / exocytic vesicle / negative regulation of smooth muscle cell apoptotic process / cell activation / positive regulation of calcineurin-NFAT signaling cascade / positive regulation of transcription regulatory region DNA binding / alphav-beta3 integrin-IGF-1-IGF1R complex / positive regulation of Ras protein signal transduction / myoblast differentiation / muscle organ development / positive regulation of insulin-like growth factor receptor signaling pathway / myoblast proliferation / negative regulation of interleukin-1 beta production / negative regulation of amyloid-beta formation / positive regulation of activated T cell proliferation / positive regulation of cardiac muscle hypertrophy / positive regulation of smooth muscle cell migration / negative regulation of release of cytochrome c from mitochondria / negative regulation of tumor necrosis factor production / epithelial to mesenchymal transition / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of glycogen biosynthetic process / positive regulation of DNA binding / positive regulation of osteoblast differentiation / SHC-related events triggered by IGF1R / 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 / insulin-like growth factor receptor signaling pathway / platelet alpha granule lumen / skeletal system development / positive regulation of epithelial cell proliferation / positive regulation of protein secretion / negative regulation of extrinsic apoptotic signaling pathway / positive regulation of glucose import / regulation of protein phosphorylation / positive regulation of smooth muscle cell proliferation / growth factor activity / wound healing / insulin receptor binding / hormone activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / cellular response to amyloid-beta / positive regulation of fibroblast proliferation / positive regulation of peptidyl-tyrosine phosphorylation / integrin binding / Platelet degranulation / response to heat / regulation of gene expression / Ras protein signal transduction / cell population proliferation / positive regulation of MAPK cascade / positive regulation of ERK1 and ERK2 cascade / protein stabilization / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of cell migration / negative regulation of gene expression / positive regulation of cell population proliferation / positive regulation of gene expression / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / signal transduction / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region
Similarity search - Function
Insulin-like growth factor I / Insulin-like, subunit E / Insulin-like / Insulin-like growth factor / Insulin family / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin family signature. / Insulin-like / Insulin / insulin-like growth factor / relaxin family. ...Insulin-like growth factor I / Insulin-like, subunit E / Insulin-like / Insulin-like growth factor / Insulin family / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin family signature. / Insulin-like / Insulin / insulin-like growth factor / relaxin family. / Insulin-like superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Insulin-like growth factor I / Insulin-like growth factor I
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsCooke, R.M. / Harvey, T.S. / Campbell, I.D.
CitationJournal: Biochemistry / Year: 1991
Title: Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study.
Authors: Cooke, R.M. / Harvey, T.S. / Campbell, I.D.
History
DepositionJan 23, 1991Processing site: BNL
Revision 1.0Apr 15, 1993Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: INSULIN-LIKE GROWTH FACTOR I


Theoretical massNumber of molelcules
Total (without water)7,6641
Polymers7,6641
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein INSULIN-LIKE GROWTH FACTOR I / Insulin-like growth factor 1


Mass: 7663.752 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P01343, UniProt: P05019*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR softwareName: GROMOS / Developer: VAN GUNSTEREN,BERENDSEN / Classification: refinement
NMR ensembleConformers submitted total number: 1

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