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- PDB-3egf: SOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR DETERMINED B... -

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Basic information

Entry
Database: PDB / ID: 3egf
TitleSOLUTION STRUCTURE OF MURINE EPIDERMAL GROWTH FACTOR DETERMINED BY NMR SPECTROSCOPY AND REFINED BY ENERGY MINIMIZATION WITH RESTRAINTS
ComponentsEPIDERMAL GROWTH FACTOR
KeywordsGROWTH 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 / positive regulation of hyaluronan biosynthetic process / negative regulation of secretion / negative regulation of cholesterol efflux / Extra-nuclear estrogen signaling / regulation of protein transport / RAF/MAP kinase cascade / PIP3 activates AKT signaling / positive regulation of epithelial tube formation / positive regulation of cerebellar granule cell precursor proliferation / Cargo recognition for clathrin-mediated endocytosis / regulation of protein localization to cell surface / positive regulation of protein localization to early endosome / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Platelet degranulation / cerebellar granule cell precursor proliferation / Clathrin-mediated endocytosis / regulation of calcium ion import / transmembrane receptor protein tyrosine kinase activator activity / positive regulation of ubiquitin-dependent protein catabolic process / epidermal growth factor receptor binding / regulation of receptor signaling pathway via JAK-STAT / positive regulation of DNA binding / ERBB2-EGFR signaling pathway / branching morphogenesis of an epithelial tube / positive regulation of receptor internalization / positive regulation of phosphorylation / mammary gland alveolus development / ERK1 and ERK2 cascade / positive regulation of endothelial cell proliferation / positive regulation of endothelial cell migration / positive regulation of mitotic nuclear division / guanyl-nucleotide exchange factor activity / epithelial cell proliferation / positive regulation of epithelial cell proliferation / growth factor activity / epidermal growth factor receptor signaling pathway / positive regulation of canonical Wnt signaling pathway / angiogenesis / cell population proliferation / 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 / 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 1. / EGF-like domain signature 2. / EGF-like domain / Ribbon / Mainly Beta
Similarity search - Domain/homology
Pro-epidermal growth factor
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR
AuthorsMontelione, G.T. / Wuthrich, K. / Scheraga, H.A.
Citation
Journal: Biochemistry / Year: 1992
Title: Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints.
Authors: Montelione, G.T. / Wuthrich, K. / Burgess, A.W. / Nice, E.C. / Wagner, G. / Gibson, K.D. / Scheraga, H.A.
#1: Journal: Biochemistry / Year: 1988
Title: Sequence-Specific 1H NMR Assignments and Identification of Slowly Exchanging Amide Protons in Murine Epidermal Growth Factor
Authors: Montelione, G.T. / Wuthrich, K. / Scheraga, H.A.
#2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1987
Title: Solution Structure of Murine Epidermal Growth Factor: Determination of the Polypeptide Backbone Chain-Fold by Nuclear Magnetic Resonance and Distance Geometry
Authors: Montelione, G.T. / Wuthrich, K. / Nice, E.C. / Burgess, A.W. / Scheraga, H.A.
#3: Journal: Proc.Natl.Acad.Sci.USA / Year: 1986
Title: Identification of Two Anti-Parallel Beta-Sheet Conformations in the Solution Structure of Murine Epidermal Growth Factor by Proton Magnetic Resonance
Authors: Montelione, G.T. / Wuthrich, K. / Nice, E.C. / Burgess, A.W. / Scheraga, H.A.
History
DepositionAug 30, 1992Processing site: BNL
Revision 1.0Jan 31, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 25, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 16, 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 1.4Oct 23, 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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MolmilJmol/JSmol

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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_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)16 / -
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

NMR software
NameDeveloperClassification
DISMANBRAUN,GOrefinement
ECEPP/2NEMETHYrefinement
NMR ensembleConformers submitted total number: 16

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