[English] 日本語
Yorodumi
- PDB-1p9j: Solution structure and dynamics of the EGF/TGF-alpha chimera T1E -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1p9j
TitleSolution structure and dynamics of the EGF/TGF-alpha chimera T1E
Componentschimera of Epidermal growth factor(EGF) and Transforming growth factor alpha (TGF-alpha)
KeywordsHORMONE/GROWTH FACTOR / chimera / EGF / TGF-alpha / ErbB1 / ErbB3 / HORMONE-GROWTH FACTOR COMPLEX
Function / homology
Function and homology information


negative regulation of secretion / positive regulation of hyaluronan biosynthetic process / negative regulation of cholesterol efflux / hepatocyte proliferation / positive regulation of cerebellar granule cell precursor proliferation / cerebellar granule cell precursor proliferation / positive regulation of epithelial tube formation / positive regulation of protein localization to early endosome / regulation of protein localization to cell surface / regulation of calcium ion import ...negative regulation of secretion / positive regulation of hyaluronan biosynthetic process / negative regulation of cholesterol efflux / hepatocyte proliferation / positive regulation of cerebellar granule cell precursor proliferation / cerebellar granule cell precursor proliferation / positive regulation of epithelial tube formation / positive regulation of protein localization to early endosome / regulation of protein localization to cell surface / regulation of calcium ion import / transmembrane receptor protein tyrosine kinase activator activity / Cargo concentration in the ER / Developmental Lineage of Pancreatic Acinar Cells / positive regulation of ubiquitin-dependent protein catabolic process / regulation of receptor signaling pathway via JAK-STAT / Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin / COPII-mediated vesicle transport / epidermal growth factor receptor binding / Inhibition of Signaling by Overexpressed EGFR / EGFR interacts with phospholipase C-gamma / NFE2L2 regulating tumorigenic genes / positive regulation of DNA binding / PLCG1 events in ERBB2 signaling / positive regulation of peptidyl-threonine phosphorylation / ERBB2-EGFR signaling pathway / branching morphogenesis of an epithelial tube / ERBB2 Activates PTK6 Signaling / Signaling by EGFR / ERBB2 Regulates Cell Motility / Signaling by ERBB4 / positive regulation of cell division / positive regulation of receptor internalization / PI3K events in ERBB2 signaling / mammary gland alveolus development / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / GAB1 signalosome / positive regulation of phosphorylation / positive regulation of endothelial cell proliferation / Signaling by ERBB2 / GRB2 events in EGFR signaling / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / SHC1 events in EGFR signaling / positive regulation of endothelial cell migration / endoplasmic reticulum-Golgi intermediate compartment membrane / ERK1 and ERK2 cascade / GRB2 events in ERBB2 signaling / positive regulation of mitotic nuclear division / SHC1 events in ERBB2 signaling / platelet alpha granule lumen / guanyl-nucleotide exchange factor activity / positive regulation of epithelial cell proliferation / epithelial cell proliferation / NOTCH3 Activation and Transmission of Signal to the Nucleus / growth factor activity / EGFR downregulation / Signaling by ERBB2 TMD/JMD mutants / clathrin-coated endocytic vesicle membrane / ER to Golgi transport vesicle membrane / Constitutive Signaling by EGFRvIII / Signaling by ERBB2 ECD mutants / Signaling by ERBB2 KD Mutants / epidermal growth factor receptor signaling pathway / Downregulation of ERBB2 signaling / Constitutive Signaling by Aberrant PI3K in Cancer / positive regulation of canonical Wnt signaling pathway / Platelet degranulation / Cargo recognition for clathrin-mediated endocytosis / PIP3 activates AKT signaling / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / Clathrin-mediated endocytosis / RAF/MAP kinase cascade / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / cytoplasmic vesicle / basolateral plasma membrane / angiogenesis / Estrogen-dependent gene expression / Extra-nuclear estrogen signaling / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / cell surface receptor signaling pathway / positive regulation of MAPK cascade / intracellular signal transduction / positive regulation of cell migration / receptor ligand activity / lysosomal membrane / positive regulation of cell population proliferation / calcium ion binding / positive regulation of gene expression / endoplasmic reticulum membrane / positive regulation of DNA-templated transcription / perinuclear region of cytoplasm / cell surface / 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 / Protransforming growth factor alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / distance geometry, brief molecular dynamics run in water.
AuthorsWingens, M. / Walma, T. / Van Ingen, H. / Stortelers, C. / Van Leeuwen, J.E. / Van Zoelen, E.J. / Vuister, G.W.
CitationJournal: J.Biol.Chem. / Year: 2003
Title: Structural Analysis of an Epidermal Growth Factor/Transforming Growth Factor-alpha Chimera with Unique ErbB Binding Specificity.
Authors: Wingens, M. / Walma, T. / Van Ingen, H. / Stortelers, C. / Van Leeuwen, J.E. / Van Zoelen, E.J. / Vuister, G.W.
History
DepositionMay 12, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 7, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 5, 2020Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _pdbx_database_status.status_code_cs
Revision 1.4Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
Revision 1.5Nov 13, 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

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: chimera of Epidermal growth factor(EGF) and Transforming growth factor alpha (TGF-alpha)


Theoretical massNumber of molelcules
Total (without water)6,3391
Polymers6,3391
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)36 / 98structures with the lowest energy
RepresentativeModel #1lowest energy

-
Components

#1: Protein chimera of Epidermal growth factor(EGF) and Transforming growth factor alpha (TGF-alpha)


Mass: 6339.224 Da / Num. of mol.: 1 / Fragment: TGF-alpha (residues 1-7), EGF (residues 8-54)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TGF-alpha and EGF / Production host: Pichia pastoris (fungus) / Strain (production host): X33 / References: UniProt: P01135, UniProt: P01133
Has protein modificationY

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1213D 15N-separated NOESY

-
Sample preparation

DetailsContents: 0.8mM T1E, 15N-labelled, 50mM phosphate buffer, 95% H20, 5%D20, pH 6.3, 20ug/mL pefabloc
Solvent system: 95% H20, 5%D20, pH 6.3
Sample conditionsIonic strength: 50 / pH: 6.3 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

-
NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA8001
Varian INOVAVarianINOVA6002

-
Processing

NMR software
NameVersionDeveloperClassification
NMRPipe203Delaglio, F.processing
X-PLOR3.851Brunger, A.refinement
CHARMM22MacKerell, A.D.refinement
RefinementMethod: distance geometry, brief molecular dynamics run in water.
Software ordinal: 1
Details: The structures are based on 660 are NOE-derived distance constraints, 98 dihedral angle restraints, and 9 distance restraints from hydrogen bonds.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 98 / Conformers submitted total number: 36

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more