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- PDB-1igl: SOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR II RELATIO... -

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Entry
Database: PDB / ID: 1igl
TitleSOLUTION STRUCTURE OF HUMAN INSULIN-LIKE GROWTH FACTOR II RELATIONSHIP TO RECEPTOR AND BINDING PROTEIN INTERACTIONS
ComponentsINSULIN-LIKE GROWTH FACTOR II
KeywordsGROWTH FACTOR
Function / homology
Function and homology information


embryonic placenta morphogenesis / positive regulation of skeletal muscle tissue growth / negative regulation of muscle cell differentiation / regulation of muscle cell differentiation / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / IRS-related events triggered by IGF1R / positive regulation of organ growth / genomic imprinting / transmembrane receptor protein tyrosine kinase activator activity / positive regulation of multicellular organism growth ...embryonic placenta morphogenesis / positive regulation of skeletal muscle tissue growth / negative regulation of muscle cell differentiation / regulation of muscle cell differentiation / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / IRS-related events triggered by IGF1R / positive regulation of organ growth / genomic imprinting / transmembrane receptor protein tyrosine kinase activator activity / positive regulation of multicellular organism growth / exocrine pancreas development / positive regulation of vascular endothelial cell proliferation / positive regulation of activated T cell proliferation / positive regulation of cell division / positive regulation of insulin receptor signaling pathway / positive regulation of glycogen biosynthetic process / embryonic placenta development / SHC-related events triggered by IGF1R / insulin-like growth factor receptor binding / striated muscle cell differentiation / positive regulation of mitotic nuclear division / insulin-like growth factor receptor signaling pathway / platelet alpha granule lumen / animal organ morphogenesis / protein serine/threonine kinase activator activity / insulin receptor binding / growth factor activity / hormone activity / integrin binding / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / glucose metabolic process / osteoblast differentiation / insulin receptor signaling pathway / Platelet degranulation / in utero embryonic development / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of MAPK cascade / 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
Insulin-like growth factor II E-peptide, C-terminal / Insulin-like growth factor II / Insulin-like growth factor II E-peptide / Insulin-like, subunit E / Insulin-like / Insulin-like growth factor / Insulin family / Insulin-like / Insulin/IGF/Relaxin family / Insulin / insulin-like growth factor / relaxin family. ...Insulin-like growth factor II E-peptide, C-terminal / Insulin-like growth factor II / Insulin-like growth factor II E-peptide / Insulin-like, subunit E / Insulin-like / Insulin-like growth factor / Insulin family / Insulin-like / Insulin/IGF/Relaxin family / Insulin / insulin-like growth factor / relaxin family. / Insulin, conserved site / Insulin family signature. / Insulin-like superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Insulin-like growth factor 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsTorres, A.M. / Forbes, B.E. / Aplin, S.E. / Wallace, J.C. / Francis, G.L. / Norton, R.S.
Citation
Journal: J.Mol.Biol. / Year: 1995
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: Journal: Eur.J.Biochem. / Year: 1990
Title: Insulin-Like Growth Factors I and II
Authors: Humbel, R.E.
#2: Journal: FED.PROC. / Year: 1983
Title: Tertiary Structures, Receptor Binding, and Antigenicity of Insulinlike Growth Factors
Authors: Blundell, T.L. / Bedarkar, S. / Humbel, R.E.
#3: Journal: Proc.Natl.Acad.Sci.USA / Year: 1978
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.
History
DepositionDec 29, 1994Processing site: BNL
Revision 1.0Feb 14, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Oct 30, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure viewerMolecule:
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Assembly

Deposited unit
A: INSULIN-LIKE GROWTH FACTOR II


Theoretical massNumber of molelcules
Total (without water)7,4841
Polymers7,4841
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
Atom site foot note1: 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
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein INSULIN-LIKE GROWTH FACTOR II


Mass: 7484.472 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P01344
Has protein modificationY

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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

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
NMR softwareName: X-PLOR / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 20

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