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- PDB-1epg: THREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE STRUCTURES OF MOUSE ... -

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Entry
Database: PDB / ID: 1epg
TitleTHREE-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE STRUCTURES OF MOUSE EPIDERMAL GROWTH FACTOR IN ACIDIC AND PHYSIOLOGICAL PH SOLUTIONS
ComponentsEPIDERMAL GROWTH FACTOR
KeywordsEPIDERMAL GROWTH FACTOR
Function / homology
Function and homology information


Signaling by ERBB4 / EGFR interacts with phospholipase C-gamma / ERBB2 Activates PTK6 Signaling / Signaling by EGFR / PI3K events in ERBB2 signaling / SHC1 events in ERBB2 signaling / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / Signaling by ERBB2 / GAB1 signalosome ...Signaling by ERBB4 / EGFR interacts with phospholipase C-gamma / ERBB2 Activates PTK6 Signaling / Signaling by EGFR / PI3K events in ERBB2 signaling / SHC1 events in ERBB2 signaling / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / Signaling by ERBB2 / GAB1 signalosome / ERBB2 Regulates Cell Motility / NOTCH3 Activation and Transmission of Signal to the Nucleus / Downregulation of ERBB2 signaling / EGFR downregulation / negative regulation of secretion / regulation of protein transport / negative regulation of cholesterol efflux / positive regulation of hyaluronan biosynthetic process / Extra-nuclear estrogen signaling / positive regulation of cerebellar granule cell precursor proliferation / RAF/MAP kinase cascade / cerebellar granule cell precursor proliferation / PIP3 activates AKT signaling / positive regulation of epithelial tube formation / Platelet degranulation / positive regulation of protein localization to early endosome / Cargo recognition for clathrin-mediated endocytosis / regulation of calcium ion import / regulation of protein localization to cell surface / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Clathrin-mediated endocytosis / positive regulation of ubiquitin-dependent protein catabolic process / regulation of receptor signaling pathway via JAK-STAT / ERBB2-EGFR signaling pathway / epidermal growth factor receptor binding / positive regulation of DNA biosynthetic process / branching morphogenesis of an epithelial tube / positive regulation of DNA binding / transmembrane receptor protein tyrosine kinase activator activity / positive regulation of receptor internalization / mammary gland alveolus development / regulation of peptidyl-tyrosine phosphorylation / positive regulation of endothelial cell proliferation / ERK1 and ERK2 cascade / positive regulation of endothelial cell migration / positive regulation of mitotic nuclear division / positive regulation of epithelial cell proliferation / epithelial cell proliferation / guanyl-nucleotide exchange factor activity / positive regulation of peptidyl-threonine phosphorylation / growth factor activity / epidermal growth factor receptor signaling pathway / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of fibroblast proliferation / positive regulation of canonical Wnt signaling pathway / angiogenesis / cell population proliferation / positive regulation of MAPK cascade / positive regulation of ERK1 and ERK2 cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor ligand activity / positive regulation of cell population proliferation / calcium ion binding / positive regulation of gene expression / positive regulation of DNA-templated transcription / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Pro-epidermal growth factor / : / Low-density lipoprotein receptor repeat class B / LDL-receptor class B (LDLRB) repeat profile. / LDLR class B repeat / Low-density lipoprotein-receptor YWTD domain / : / Calcium-binding EGF domain / Six-bladed beta-propeller, TolB-like / Laminin ...Pro-epidermal growth factor / : / Low-density lipoprotein receptor repeat class B / LDL-receptor class B (LDLRB) repeat profile. / LDLR class B repeat / Low-density lipoprotein-receptor YWTD domain / : / Calcium-binding EGF domain / Six-bladed beta-propeller, TolB-like / Laminin / Laminin / Coagulation Factor Xa inhibitory site / EGF-like domain / EGF-type aspartate/asparagine hydroxylation site / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / Epidermal growth factor-like domain. / EGF-like domain profile. / Growth factor receptor cysteine-rich domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1. / EGF-like domain / Ribbon / Mainly Beta
Similarity search - Domain/homology
Pro-epidermal growth factor
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR
AuthorsKohda, D. / Inagaki, F.
Citation
Journal: Biochemistry / Year: 1992
Title: Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions.
Authors: Kohda, D. / Inagaki, F.
#1: Journal: Biochemistry / Year: 1992
Title: Structure of Epidermal Growth Factor Bound to Perdeuterated Dodecylphosphocholine Micelles Determined by Two-Dimensional NMR and Simulated Annealing Calculations
Authors: Kohda, D. / Inagaki, F.
#2: Journal: Biochemistry / Year: 1991
Title: Characterization of Ph Titration Shifts for All the Nonlabile Proton Resonances in a Protein by Two-Dimensional NMR: The Case of Mouse Epidermal Growth Factor
Authors: Kohda, D. / Sawada, T. / Inagaki, F.
#3: Journal: J.Biochem.(Tokyo) / Year: 1988
Title: Tertiary Structure of Mouse Epidermal Growth Factor Determined by Two-Dimensional 1H NMR
Authors: Kohda, D. / Go, N. / Hayashi, K. / Inagaki, F.
#4: Journal: Biochem.Int. / Year: 1988
Title: A Comparative 1H NMR Study of Mouse Alpha(1-53) and Beta(2-53) Epidermal Growth Factors
Authors: Kohda, D. / Kodama, C. / Kase, R. / Nomoto, H. / Hayashi, K. / Inagaki, F.
#5: Journal: J.Biochem.(Tokyo) / Year: 1988
Title: Complete Sequence-Specific 1H Nuclear Magnetic Resonance Assignments for Mouse Epidermal Growth Factor
Authors: Kohda, D. / Inagaki, F.
History
DepositionMar 24, 1992Processing site: BNL
Revision 1.0Jan 31, 1994Provider: 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
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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Assembly

Deposited unit
A: EPIDERMAL GROWTH FACTOR


Theoretical massNumber of molelcules
Total (without water)6,0511
Polymers6,0511
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / -
Representative

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Components

#1: Protein EPIDERMAL GROWTH FACTOR


Mass: 6050.717 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / References: UniProt: P01132
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: 1

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