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- PDB-1mfl: The Structure of ERBIN PDZ domain bound to the Carboxy-terminal t... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mfl | ||||||
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Title | The Structure of ERBIN PDZ domain bound to the Carboxy-terminal tail of the ErbB2 Receptor | ||||||
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![]() | SIGNALING PROTEIN / PDZ DOMAIN / PHOSPHORYLATION / ERB-B2 / ERBIN | ||||||
Function / homology | ![]() basal protein localization / ErbB-2 class receptor binding / negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / hemidesmosome / neurotransmitter receptor transport postsynaptic membrane to endosome / negative regulation of immature T cell proliferation in thymus / ERBB3:ERBB2 complex / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling / immature T cell proliferation in thymus ...basal protein localization / ErbB-2 class receptor binding / negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / hemidesmosome / neurotransmitter receptor transport postsynaptic membrane to endosome / negative regulation of immature T cell proliferation in thymus / ERBB3:ERBB2 complex / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling / immature T cell proliferation in thymus / RNA polymerase I core binding / embryo development / neurotransmitter receptor transport, endosome to postsynaptic membrane / intermediate filament cytoskeleton organization / negative regulation of monocyte chemotactic protein-1 production / regulation of microtubule-based process / ErbB-3 class receptor binding / semaphorin receptor complex / Sema4D induced cell migration and growth-cone collapse / establishment or maintenance of epithelial cell apical/basal polarity / motor neuron axon guidance / neurotransmitter receptor localization to postsynaptic specialization membrane / PLCG1 events in ERBB2 signaling / neuromuscular junction development / ERBB2-EGFR signaling pathway / RHOB GTPase cycle / ERBB2 Activates PTK6 Signaling / positive regulation of Rho protein signal transduction / Drug-mediated inhibition of ERBB2 signaling / Resistance of ERBB2 KD mutants to trastuzumab / Resistance of ERBB2 KD mutants to sapitinib / Resistance of ERBB2 KD mutants to tesevatinib / Resistance of ERBB2 KD mutants to neratinib / Resistance of ERBB2 KD mutants to osimertinib / Resistance of ERBB2 KD mutants to afatinib / Resistance of ERBB2 KD mutants to AEE788 / Resistance of ERBB2 KD mutants to lapatinib / Drug resistance in ERBB2 TMD/JMD mutants / enzyme-linked receptor protein signaling pathway / negative regulation of NF-kappaB transcription factor activity / positive regulation of transcription by RNA polymerase I / ERBB2-ERBB3 signaling pathway / RHOC GTPase cycle / oligodendrocyte differentiation / receptor clustering / ERBB2 Regulates Cell Motility / response to muramyl dipeptide / semaphorin-plexin signaling pathway / PI3K events in ERBB2 signaling / positive regulation of cell adhesion / RHOG GTPase cycle / basement membrane / RHOA GTPase cycle / positive regulation of protein targeting to membrane / RAC2 GTPase cycle / RAC3 GTPase cycle / protein targeting / regulation of angiogenesis / coreceptor activity / Schwann cell development / Signaling by ERBB2 / cellular response to epidermal growth factor stimulus / cell surface receptor protein tyrosine kinase signaling pathway / RAC1 GTPase cycle / GRB2 events in ERBB2 signaling / myelination / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / Downregulation of ERBB2:ERBB3 signaling / transmembrane receptor protein tyrosine kinase activity / SHC1 events in ERBB2 signaling / Constitutive Signaling by Overexpressed ERBB2 / phosphatidylinositol 3-kinase/protein kinase B signal transduction / neurogenesis / regulation of ERK1 and ERK2 cascade / basal plasma membrane / positive regulation of epithelial cell proliferation / positive regulation of translation / integrin-mediated signaling pathway / adherens junction / Signaling by ERBB2 TMD/JMD mutants / positive regulation of MAP kinase activity / wound healing / Signaling by ERBB2 ECD mutants / neuromuscular junction / neuron differentiation / Signaling by ERBB2 KD Mutants / epidermal growth factor receptor signaling pathway / receptor protein-tyrosine kinase / structural constituent of cytoskeleton / receptor tyrosine kinase binding / cellular response to growth factor stimulus / Downregulation of ERBB2 signaling / ruffle membrane / cell-cell adhesion / peptidyl-tyrosine phosphorylation / transmembrane signaling receptor activity / Constitutive Signaling by Aberrant PI3K in Cancer / cell junction / PIP3 activates AKT signaling / myelin sheath Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Birrane, G. / Chung, J. / Ladias, J.A. | ||||||
![]() | ![]() Title: Novel mode of ligand recognition by the erbin PDZ domain Authors: Birrane, G. / Chung, J. / Ladias, J.A. #1: ![]() Title: BIN: A BASOLATERAL PDZ PROTEIN THAT INTERACTS WITH THE MAMMALIAN ERBB2/HER2 RECEPTOR Authors: BORG, J.P. / MARCHETTO, S. / LEBIVIC, A. / OLLENDORFF, V. / JAULIN-BASTARD, F. / SAITO, H. / FOURNIER, E. / ADELAIDE, J. / MARGOLIS, B. / BIRNBAUM, D. #2: ![]() Title: THE ERBIN PDZ DOMAIN BINDS WITH HIGH AFFINITY AND SPECIFICITY TO THE CARBOXYL TERMINI OF DELTA-CATENIN AND ARVCF Authors: LAURA, R.P. / WITT, A.S. / HELD, H.A. / GERSTNER, R. / DESHAYES, K. / KOEHLER, M.F. / KOSIK, K.S. / SIDHU, S.S. / LASKY, L.A. #3: ![]() Title: ERBIN IS A PROTEIN CONCENTRATED AT POSTSYNAPTIC MEMBRANES THAT INTERACTS WITH PSD-95 Authors: HUANG, Y.Z. / WANG, Q. / XIONG, W.C. / MEI, L. #4: ![]() Title: THE ERBB2/HER2 RECEPTOR DIFFERENTIALLY INTERACTS WITH ERBIN AND PICK1 PSD-95/DLG/ZO-1 DOMAIN PROTEINS Authors: JAULIN-BASTARD, F. / SAITO, H. / LEBIVIC, A. / OLLENDORFF, V. / MARCHETTO, S. / BIRNBAUM, D. / BORG, J.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 33.5 KB | Display | ![]() |
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PDB format | ![]() | 22.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.4 KB | Display | ![]() |
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Full document | ![]() | 425.3 KB | Display | |
Data in XML | ![]() | 6.7 KB | Display | |
Data in CIF | ![]() | 8.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1mfgSC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 10292.593 Da / Num. of mol.: 1 / Fragment: PDZ DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1084.113 Da / Num. of mol.: 1 / Fragment: PEPTIDE LDVPV / Source method: obtained synthetically / Details: PEPTIDE SYNTHESIZED CHEMICALLY / References: UniProt: P04626*PLUS |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.38 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 4.5 Details: 23-26% PEG 4000, 20% GLYCEROL, 100mM AMMONIUM ACETATE, 100mM SODIUM ACETATE, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 8.3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 4, 2002 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.88→30.6 Å / Num. all: 7196 / Num. obs: 7068 / % possible obs: 95 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3.73 % / Biso Wilson estimate: 13 Å2 / Rmerge(I) obs: 0.028 / Rsym value: 0.028 / Net I/σ(I): 44.7 |
Reflection shell | Resolution: 1.88→1.95 Å / Redundancy: 3.34 % / Rmerge(I) obs: 0.096 / Mean I/σ(I) obs: 13.3 / Num. unique all: 660 / Rsym value: 0.096 / % possible all: 90.2 |
Reflection shell | *PLUS Lowest resolution: 1.93 Å / % possible obs: 90.2 % |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1MFG Resolution: 1.88→30.57 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.941 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.168 Å2
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Refinement step | Cycle: LAST / Resolution: 1.88→30.57 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.88→1.929 Å / Total num. of bins used: 20 /
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Refinement | *PLUS Lowest resolution: 30.6 Å / Num. reflection obs: 6737 / % reflection Rfree: 5 % / Rfactor Rfree: 0.216 / Rfactor Rwork: 0.167 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |