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- PDB-3u2p: Crystal structure of N-terminal three extracellular domains of Er... -

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Basic information

Entry
Database: PDB / ID: 3u2p
TitleCrystal structure of N-terminal three extracellular domains of ErbB4/Her4
ComponentsReceptor tyrosine-protein kinase erbB-4
KeywordsTransferase / Signaling protein / Cell surface receptor / Signaling
Function / homology
Function and homology information


establishment of planar polarity involved in nephron morphogenesis / ERBB4 signaling pathway / ERBB4-ERBB4 signaling pathway / olfactory bulb interneuron differentiation / central nervous system morphogenesis / neuregulin receptor activity / cardiac muscle tissue regeneration / negative regulation of neuron migration / ERBB2-ERBB4 signaling pathway / mitochondrial fragmentation involved in apoptotic process ...establishment of planar polarity involved in nephron morphogenesis / ERBB4 signaling pathway / ERBB4-ERBB4 signaling pathway / olfactory bulb interneuron differentiation / central nervous system morphogenesis / neuregulin receptor activity / cardiac muscle tissue regeneration / negative regulation of neuron migration / ERBB2-ERBB4 signaling pathway / mitochondrial fragmentation involved in apoptotic process / GABA receptor binding / PI3K events in ERBB4 signaling / mammary gland epithelial cell differentiation / embryonic pattern specification / positive regulation of protein localization to cell surface / neural crest cell migration / epidermal growth factor receptor binding / positive regulation of tyrosine phosphorylation of STAT protein / neurotransmitter receptor localization to postsynaptic specialization membrane / ERBB2 Activates PTK6 Signaling / ERBB2 Regulates Cell Motility / Signaling by ERBB4 / Long-term potentiation / PI3K events in ERBB2 signaling / mammary gland alveolus development / SHC1 events in ERBB4 signaling / cell surface receptor signaling pathway via JAK-STAT / cell fate commitment / Nuclear signaling by ERBB4 / synapse assembly / positive regulation of cardiac muscle cell proliferation / Signaling by ERBB2 / transmembrane receptor protein tyrosine kinase activity / lactation / GRB2 events in ERBB2 signaling / Downregulation of ERBB4 signaling / SHC1 events in ERBB2 signaling / cellular response to epidermal growth factor stimulus / cell surface receptor protein tyrosine kinase signaling pathway / regulation of cell migration / positive regulation of epithelial cell proliferation / basal plasma membrane / GABA-ergic synapse / positive regulation of receptor signaling pathway via JAK-STAT / Signaling by ERBB2 TMD/JMD mutants / placental growth factor receptor activity / postsynaptic density membrane / insulin receptor activity / vascular endothelial growth factor receptor activity / hepatocyte growth factor receptor activity / macrophage colony-stimulating factor receptor activity / platelet-derived growth factor alpha-receptor activity / platelet-derived growth factor beta-receptor activity / stem cell factor receptor activity / boss receptor activity / protein tyrosine kinase collagen receptor activity / brain-derived neurotrophic factor receptor activity / transmembrane-ephrin receptor activity / GPI-linked ephrin receptor activity / epidermal growth factor receptor activity / fibroblast growth factor receptor activity / insulin-like growth factor receptor activity / receptor protein-tyrosine kinase / neuromuscular junction / peptidyl-tyrosine phosphorylation / Signaling by ERBB2 KD Mutants / epidermal growth factor receptor signaling pathway / Downregulation of ERBB2 signaling / neuron differentiation / Constitutive Signaling by Aberrant PI3K in Cancer / cell migration / nervous system development / PIP3 activates AKT signaling / positive regulation of protein phosphorylation / presynaptic membrane / heart development / RAF/MAP kinase cascade / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / protein autophosphorylation / protein tyrosine kinase activity / basolateral plasma membrane / Estrogen-dependent gene expression / postsynaptic membrane / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / positive regulation of ERK1 and ERK2 cascade / transcription cis-regulatory region binding / positive regulation of MAPK cascade / mitochondrial matrix / negative regulation of cell population proliferation / positive regulation of cell population proliferation / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / glutamatergic synapse / signal transduction / protein homodimerization activity / mitochondrion / extracellular region / nucleoplasm / ATP binding
Similarity search - Function
Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / : / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Alpha-Beta Horseshoe ...Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / : / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Alpha-Beta Horseshoe / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain / Furin-like repeat / Furin-like repeats / Growth factor receptor cysteine-rich domain superfamily / : / Ribbon / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Receptor tyrosine-protein kinase erbB-4
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.57 Å
AuthorsLiu, P. / Bouyain, S. / Elgenbrot, C. / Leahy, D.J.
CitationJournal: Protein Sci. / Year: 2012
Title: The ErbB4 extracellular region retains a tethered-like conformation in the absence of the tether.
Authors: Liu, P. / Bouyain, S. / Eigenbrot, C. / Leahy, D.J.
History
DepositionOct 4, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 9, 2011Provider: repository / Type: Initial release
Revision 1.1Oct 3, 2012Group: Database references
Revision 1.2Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Receptor tyrosine-protein kinase erbB-4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,5776
Polymers55,4711
Non-polymers1,1065
Water1,54986
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)42.170, 85.560, 152.400
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Receptor tyrosine-protein kinase erbB-4 / Proto-oncogene-like protein c-ErbB-4 / Tyrosine kinase-type cell surface receptor HER4 / p180erbB4 ...Proto-oncogene-like protein c-ErbB-4 / Tyrosine kinase-type cell surface receptor HER4 / p180erbB4 / ERBB4 Extracelluar domain / 4ICD / E4ICD / s80HER4


Mass: 55470.703 Da / Num. of mol.: 1 / Fragment: unp residues 26-522
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ERBB4, HER4 / Production host: Cricetulus griseus (Chinese hamster) / Strain (production host): Lec1
References: UniProt: Q15303, receptor protein-tyrosine kinase
#2: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 86 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.48 Å3/Da / Density % sol: 50.37 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 16% PEG8000,0.2M Calcium acetate, 0.1M Socium Cacodylate, VAPOR DIFFUSION, HANGING DROP, temperature 293K, pH 6.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU FR-E+ SUPERBRIGHT / Wavelength: 1.5418 Å
DetectorType: RIGAKU SATURN 944+ / Detector: CCD / Date: Sep 30, 2009
RadiationMonochromator: Varimax VHF / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.57→50 Å / Num. all: 17809 / Num. obs: 17809 / % possible obs: 97.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.2 % / Biso Wilson estimate: 61.99 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 10.2
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allDiffraction-ID% possible all
2.57-2.664.60.4721755197.2
2.66-2.775.40.3651728196.5
2.77-2.895.30.2821733196.9
2.89-3.055.20.2191728195.3
3.05-3.245.20.1471717195.2
3.24-3.4950.1021719195.3
3.49-3.8450.0761777196.9
3.84-4.395.20.0641818199.3
4.39-5.535.70.0591864199.9
5.53-505.70.0611970198.3

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASERphasing
BUSTER2.8.0refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: pdb entry 2AHX

2ahx


Resolution: 2.57→24.87 Å / Cor.coef. Fo:Fc: 0.9346 / Cor.coef. Fo:Fc free: 0.9003 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.2429 920 5.18 %RANDOM
Rwork0.1923 ---
all0.1951 17758 --
obs0.1951 17758 --
Displacement parametersBiso mean: 50.33 Å2
Baniso -1Baniso -2Baniso -3
1--0.7733 Å20 Å20 Å2
2--3.0378 Å20 Å2
3----2.2645 Å2
Refine analyzeLuzzati coordinate error obs: 0.338 Å
Refinement stepCycle: LAST / Resolution: 2.57→24.87 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3737 0 70 86 3893
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.013903HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.245306HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d1319SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes108HARMONIC2
X-RAY DIFFRACTIONt_gen_planes574HARMONIC5
X-RAY DIFFRACTIONt_it3903HARMONIC20
X-RAY DIFFRACTIONt_omega_torsion3.35
X-RAY DIFFRACTIONt_other_torsion19.08
X-RAY DIFFRACTIONt_chiral_improper_torsion530SEMIHARMONIC5
X-RAY DIFFRACTIONt_ideal_dist_contact4359SEMIHARMONIC4
LS refinement shellResolution: 2.57→2.73 Å / Total num. of bins used: 9
RfactorNum. reflection% reflection
Rfree0.2894 148 5.29 %
Rwork0.2232 2649 -
all0.227 2797 -
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.33470.10310.12070.93490.86611.8373-0.0326-0.0481-0.04390.15520.0288-0.00250.02920.0010.0038-0.08620.0369-0.0007-0.1005-0.0494-0.1194-12.98297.971-14.2629
25.02821.27660.00133.9958-0.13873.44380.0855-0.0617-0.01740.0916-0.2275-0.05860.12330.10450.1419-0.21260.00760.0352-0.1624-0.0012-0.19-30.033759.1274-25.3436
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{ A|1 - A|300 }A1 - 300
2X-RAY DIFFRACTION2{ A|301 - A|497}A301 - 497

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