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- PDB-1mfg: 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: 1mfg | ||||||
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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 / PROTEIN-PEPTIDE COMPLEX / 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 / postsynaptic specialization / negative regulation of immature T cell proliferation in thymus / ERBB3:ERBB2 complex / PLCG1 events in ERBB2 signaling / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling ...basal protein localization / ErbB-2 class receptor binding / negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / hemidesmosome / postsynaptic specialization / negative regulation of immature T cell proliferation in thymus / ERBB3:ERBB2 complex / PLCG1 events in ERBB2 signaling / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling / immature T cell proliferation in thymus / RNA polymerase I core binding / ERBB2-EGFR signaling pathway / intermediate filament cytoskeleton organization / ERBB2 Activates PTK6 Signaling / semaphorin receptor complex / negative regulation of monocyte chemotactic protein-1 production / regulation of microtubule-based process / ErbB-3 class receptor binding / establishment or maintenance of epithelial cell apical/basal polarity / ERBB2 Regulates Cell Motility / Sema4D induced cell migration and growth-cone collapse / motor neuron axon guidance / PI3K events in ERBB2 signaling / neurotransmitter receptor localization to postsynaptic specialization membrane / positive regulation of Rho protein signal transduction / negative regulation of NF-kappaB transcription factor activity / RHOB GTPase cycle / neuromuscular junction development / 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 / ERBB2-ERBB3 signaling pathway / positive regulation of transcription by RNA polymerase I / RHOC GTPase cycle / oligodendrocyte differentiation / regulation of postsynaptic membrane neurotransmitter receptor levels / response to muramyl dipeptide / semaphorin-plexin signaling pathway / cellular response to epidermal growth factor stimulus / Signaling by ERBB2 / positive regulation of cell adhesion / RHOG GTPase cycle / basement membrane / RHOA GTPase cycle / positive regulation of protein targeting to membrane / RAC2 GTPase cycle / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / RAC3 GTPase cycle / GRB2 events in ERBB2 signaling / transmembrane receptor protein tyrosine kinase activity / protein targeting / regulation of angiogenesis / neurogenesis / SHC1 events in ERBB2 signaling / coreceptor activity / regulation of ERK1 and ERK2 cascade / Schwann cell development / basal plasma membrane / positive regulation of epithelial cell proliferation / cell surface receptor protein tyrosine kinase signaling pathway / RAC1 GTPase cycle / myelination / phosphatidylinositol 3-kinase/protein kinase B signal transduction / Downregulation of ERBB2:ERBB3 signaling / Constitutive Signaling by Overexpressed ERBB2 / Signaling by ERBB2 TMD/JMD mutants / positive regulation of MAP kinase activity / Signaling by ERBB2 ECD mutants / Signaling by ERBB2 KD Mutants / epidermal growth factor receptor signaling pathway / integrin-mediated signaling pathway / positive regulation of translation / receptor protein-tyrosine kinase / Downregulation of ERBB2 signaling / ruffle membrane / wound healing / neuromuscular junction / peptidyl-tyrosine phosphorylation / neuron differentiation / transmembrane signaling receptor activity / structural constituent of cytoskeleton / receptor tyrosine kinase binding / cellular response to growth factor stimulus / Constitutive Signaling by Aberrant PI3K in Cancer / cell junction / PIP3 activates AKT signaling / myelin sheath / cellular response to tumor necrosis factor / presynaptic membrane / heart development / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling 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 | ![]() | 59.6 KB | Display | ![]() |
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PDB format | ![]() | 43.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Details | COORDINATES REPRESENT THE COMPLETE BIOLOGICAL ASSEMBLY |
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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: 1004.134 Da / Num. of mol.: 1 / Fragment: PEPTIDE EYLGLDVPV / 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: 1.71 Å3/Da / Density % sol: 39.16 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 4.6 Details: 12-15%PEG 4000, 100mM Ammonium Acetate, 100mM Sodium Acetate, 10% Glycerol, pH 4.6, 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: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 10, 2002 / Details: DUAL SLITS |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97861 Å / Relative weight: 1 |
Reflection | Resolution: 1.25→25 Å / Num. all: 24313 / Num. obs: 24313 / % possible obs: 97.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 |
Reflection shell | Resolution: 1.25→1.29 Å / % possible all: 91.4 |
Reflection | *PLUS % possible obs: 92.7 % / Rmerge(I) obs: 0.025 |
Reflection shell | *PLUS % possible obs: 91.4 % / Rmerge(I) obs: 0.037 / Mean I/σ(I) obs: 16.8 |
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Processing
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Refinement | Method to determine structure: ![]() Details: ANISOTROPIC REFINEMENT REDUCED FREE R (NO CUTOFF) BY 2.6% Water molecules 131, 132 and 133 occupy the site where the disordered component of HIS1347 with alternate conformer B is modeled.
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Refine analyze | Num. disordered residues: 8 / Occupancy sum hydrogen: 766 / Occupancy sum non hydrogen: 929.08 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.25→25 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 25 Å / % reflection Rfree: 5 % / Rfactor Rfree: 0.164 / Rfactor Rwork: 0.128 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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