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- PDB-1hrf: SOLUTION STRUCTURE OF THE EPIDERMAL GROWTH FACTOR-LIKE DOMAIN OF ... -

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Entry
Database: PDB / ID: 1hrf
TitleSOLUTION STRUCTURE OF THE EPIDERMAL GROWTH FACTOR-LIKE DOMAIN OF HEREGULIN-ALPHA, A LIGAND FOR P180ERB4
ComponentsHEREGULIN ALPHA
KeywordsGROWTH FACTOR
Function / homology
Function and homology information


ERBB3 signaling pathway / positive regulation of peptidyl-tyrosine autophosphorylation / ERBB4 signaling pathway / ERBB4-ERBB4 signaling pathway / ventricular cardiac muscle cell differentiation / positive regulation of striated muscle cell differentiation / negative regulation of secretion / endocardial cell differentiation / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling ...ERBB3 signaling pathway / positive regulation of peptidyl-tyrosine autophosphorylation / ERBB4 signaling pathway / ERBB4-ERBB4 signaling pathway / ventricular cardiac muscle cell differentiation / positive regulation of striated muscle cell differentiation / negative regulation of secretion / endocardial cell differentiation / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling / neural crest cell development / cell communication / cardiac muscle cell myoblast differentiation / PI3K events in ERBB4 signaling / peripheral nervous system development / cardiac muscle cell differentiation / transmembrane receptor protein tyrosine kinase activator activity / chemorepellent activity / mammary gland development / ventricular trabecula myocardium morphogenesis / ErbB-3 class receptor binding / activation of transmembrane receptor protein tyrosine kinase activity / ERBB signaling pathway / negative regulation of cardiac muscle cell apoptotic process / ERBB2 Activates PTK6 Signaling / regulation of postsynaptic neurotransmitter receptor internalization / ERBB2-ERBB3 signaling pathway / ERBB2 Regulates Cell Motility / protein tyrosine kinase activator activity / Signaling by ERBB4 / Long-term potentiation / nickel cation binding / PI3K events in ERBB2 signaling / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / SHC1 events in ERBB4 signaling / Nuclear signaling by ERBB4 / activation of protein kinase B activity / positive regulation of cardiac muscle cell proliferation / Signaling by ERBB2 / GRB2 events in ERBB2 signaling / positive regulation of cell adhesion / SHC1 events in ERBB2 signaling / Downregulation of ERBB2:ERBB3 signaling / cell surface receptor protein tyrosine kinase signaling pathway / cytokine activity / transcription coregulator activity / positive regulation of protein-containing complex assembly / growth factor activity / wound healing / Signaling by ERBB2 TMD/JMD mutants / brain development / Signaling by ERBB2 KD Mutants / receptor tyrosine kinase binding / Downregulation of ERBB2 signaling / Constitutive Signaling by Aberrant PI3K in Cancer / integrin binding / nervous system development / PIP3 activates AKT signaling / RAF/MAP kinase cascade / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of cell growth / cell differentiation / cell population proliferation / positive regulation of ERK1 and ERK2 cascade / intracellular signal transduction / apical plasma membrane / receptor ligand activity / signaling receptor binding / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / glutamatergic synapse / extracellular space / extracellular region / zinc ion binding / nucleoplasm / membrane / plasma membrane
Similarity search - Function
Neuregulin, C-terminal / Neuregulin-1 / Neuregulin / Neuregulin intracellular region / Laminin / Laminin / EGF-like domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Epidermal growth factor-like domain. ...Neuregulin, C-terminal / Neuregulin-1 / Neuregulin / Neuregulin intracellular region / Laminin / Laminin / EGF-like domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Epidermal growth factor-like domain. / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain signature 2. / EGF-like domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Ribbon / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Mainly Beta
Similarity search - Domain/homology
Pro-neuregulin-1, membrane-bound isoform
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsNagata, K. / Kohda, D. / Hatanaka, H. / Ichikawa, S. / Inagaki, F.
CitationJournal: EMBO J. / Year: 1994
Title: Solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erbB-4.
Authors: Nagata, K. / Kohda, D. / Hatanaka, H. / Ichikawa, S. / Matsuda, S. / Yamamoto, T. / Suzuki, A. / Inagaki, F.
History
DepositionJul 21, 1994Processing site: BNL
Revision 1.0Oct 15, 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 23, 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 visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HEREGULIN ALPHA


Theoretical massNumber of molelcules
Total (without water)7,5451
Polymers7,5451
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / -
Representative

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Components

#1: Protein HEREGULIN ALPHA


Mass: 7544.686 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / References: UniProt: Q02297
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: 10

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