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- PDB-1yug: TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 15 MODELS AFTER ECEPP... -

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Entry
Database: PDB / ID: 1yug
TitleTYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 15 MODELS AFTER ECEPP/3 ENERGY MINIMIZATION
ComponentsTRANSFORMING GROWTH FACTOR ALPHA
KeywordsGROWTH FACTOR / EGF-LIKE DOMAIN STRUCTURE
Function / homology
Function and homology information


hepatocyte proliferation / transmembrane receptor protein tyrosine kinase activator activity / Cargo concentration in the ER / COPII-mediated vesicle transport / epidermal growth factor receptor binding / Inhibition of Signaling by Overexpressed EGFR / EGFR interacts with phospholipase C-gamma / ERBB2-EGFR signaling pathway / Signaling by EGFR / positive regulation of cell division ...hepatocyte proliferation / transmembrane receptor protein tyrosine kinase activator activity / Cargo concentration in the ER / COPII-mediated vesicle transport / epidermal growth factor receptor binding / Inhibition of Signaling by Overexpressed EGFR / EGFR interacts with phospholipase C-gamma / ERBB2-EGFR signaling pathway / Signaling by EGFR / positive regulation of cell division / mammary gland alveolus development / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / GAB1 signalosome / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of mitotic nuclear division / positive regulation of epithelial cell proliferation / growth factor activity / EGFR downregulation / clathrin-coated endocytic vesicle membrane / ER to Golgi transport vesicle membrane / epidermal growth factor receptor signaling pathway / Constitutive Signaling by Aberrant PI3K in Cancer / Cargo recognition for clathrin-mediated endocytosis / PIP3 activates AKT signaling / Clathrin-mediated endocytosis / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / cytoplasmic vesicle / angiogenesis / basolateral plasma membrane / Estrogen-dependent gene expression / cell surface receptor signaling pathway / Extra-nuclear estrogen signaling / positive regulation of MAPK cascade / intracellular signal transduction / receptor ligand activity / positive regulation of cell population proliferation / endoplasmic reticulum membrane / perinuclear region of cytoplasm / cell surface / extracellular space / extracellular region / plasma membrane
Similarity search - Function
Laminin / Laminin / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain signature 2. / EGF-like domain / Ribbon / Mainly Beta
Similarity search - Domain/homology
Protransforming growth factor alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsMoy, F.J. / Montelione, G.T. / Scheraga, H.A.
Citation
Journal: Biochemistry / Year: 1993
Title: Solution structure of human type-alpha transforming growth factor determined by heteronuclear NMR spectroscopy and refined by energy minimization with restraints.
Authors: Moy, F.J. / Li, Y.C. / Rauenbuehler, P. / Winkler, M.E. / Scheraga, H.A. / Montelione, G.T.
#1: Journal: J.Biomol.NMR / Year: 1995
Title: Crankshaft Motions of the Polypeptide Backbone in Molecular Dynamics Simulations of Human Type-Alpha Transforming Growth Factor
Authors: Fadel, A.R. / Jin, D.Q. / Montelione, G.T. / Levy, R.M.
#2: Journal: Biochemistry / Year: 1995
Title: Human Type-Alpha Transforming Growth Factor Undergoes Slow Conformational Exchange between Multiple Backbone Conformations as Characterized by Nitrogen-15 Relaxation Measurements
Authors: Li, Y.C. / Montelione, G.T.
#3: Journal: Proc.Natl.Acad.Sci.USA / Year: 1989
Title: Sequence-Specific 1H-NMR Assignments and Identification of Two Small Antiparallel Beta-Sheets in the Solution Structure of Recombinant Human Transforming Growth Factor Alpha
Authors: Montelione, G.T. / Winkler, M.E. / Burton, L.E. / Rinderknecht, E. / Sporn, M.B. / Wagner, G.
History
DepositionApr 1, 1996Processing site: BNL
Revision 1.0Aug 17, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 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
Revision 1.4Nov 20, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure viewerMolecule:
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Assembly

Deposited unit
A: TRANSFORMING GROWTH FACTOR ALPHA


Theoretical massNumber of molelcules
Total (without water)5,5601
Polymers5,5601
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / -
Representative

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Components

#1: Protein/peptide TRANSFORMING GROWTH FACTOR ALPHA / TGF-ALPHA / H-TGF-ALPHA


Mass: 5560.246 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HUMAN TGF-ALPHA 1YUG / Plasmid: PTE5 / Gene (production host): HUMAN TGF-ALPHA 1YUG / Production host: Escherichia coli (E. coli) / References: UniProt: P01135
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

NMR softwareName: ECEPP/3 / Developer: NEMETHY, SCHERAGA, ET AL. / Classification: refinement
NMR ensembleConformers submitted total number: 15

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