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- PDB-1i5h: SOLUTION STRUCTURE OF THE RNEDD4 WWIII DOMAIN-RENAL BP2 PEPTIDE C... -
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Basic information
Entry | Database: PDB / ID: 1i5h | ||||||
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Title | SOLUTION STRUCTURE OF THE RNEDD4 WWIII DOMAIN-RENAL BP2 PEPTIDE COMPLEX | ||||||
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![]() | LIGASE / Nedd4 / WW domains / ENaC / PY Motif / Liddle syndrome / proline-rich | ||||||
Function / homology | ![]() Downregulation of ERBB4 signaling / Stimuli-sensing channels / Regulation of PTEN localization / ISG15 antiviral mechanism / positive regulation of nucleocytoplasmic transport / Regulation of PTEN stability and activity / Antigen processing: Ubiquitination & Proteasome degradation / sodium channel complex / ligand-gated sodium channel activity / endocardial cushion development ...Downregulation of ERBB4 signaling / Stimuli-sensing channels / Regulation of PTEN localization / ISG15 antiviral mechanism / positive regulation of nucleocytoplasmic transport / Regulation of PTEN stability and activity / Antigen processing: Ubiquitination & Proteasome degradation / sodium channel complex / ligand-gated sodium channel activity / endocardial cushion development / negative regulation of sodium ion transport / response to denervation involved in regulation of muscle adaptation / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / nuclear receptor-mediated glucocorticoid signaling pathway / sodium ion homeostasis / artery smooth muscle contraction / regulation protein catabolic process at postsynapse / WW domain binding / phosphothreonine residue binding / receptor catabolic process / protein targeting to lysosome / multicellular organismal-level water homeostasis / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / plasma membrane protein complex / HECT-type E3 ubiquitin transferase / sodium channel inhibitor activity / regulation of postsynaptic neurotransmitter receptor internalization / proline-rich region binding / regulation of monoatomic ion transmembrane transport / wound healing, spreading of epidermal cells / RNA polymerase binding / blood vessel morphogenesis / postsynaptic cytosol / lysosomal transport / neuromuscular junction development / sodium ion transport / regulation of dendrite morphogenesis / regulation of synapse organization / negative regulation of vascular endothelial growth factor receptor signaling pathway / outflow tract morphogenesis / progesterone receptor signaling pathway / plasma membrane => GO:0005886 / protein monoubiquitination / microvillus / protein K63-linked ubiquitination / sodium ion transmembrane transport / phosphoserine residue binding / beta-2 adrenergic receptor binding / regulation of sodium ion transport / ubiquitin ligase complex / T cell activation / ubiquitin binding / establishment of localization in cell / regulation of membrane potential / ionotropic glutamate receptor binding / cytoplasmic vesicle membrane / receptor internalization / sensory perception of taste / positive regulation of protein catabolic process / ubiquitin-protein transferase activity / cellular response to UV / neuron projection development / ubiquitin protein ligase activity / cell cortex / ubiquitin-dependent protein catabolic process / adaptive immune response / dendritic spine / membrane => GO:0016020 / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / response to hypoxia / protein ubiquitination / immune response / apical plasma membrane / protein domain specific binding / external side of plasma membrane / innate immune response / glutamatergic synapse / DNA damage response / chromatin / perinuclear region of cytoplasm / Golgi apparatus / enzyme binding / negative regulation of transcription by RNA polymerase II / cell surface / protein-containing complex / extracellular exosome / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Kanelis, V. / Rotin, D. / Forman-Kay, J.D. | ||||||
![]() | ![]() Title: Solution structure of a Nedd4 WW domain-ENaC peptide complex. Authors: Kanelis, V. / Rotin, D. / Forman-Kay, J.D. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 303.3 KB | Display | ![]() |
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PDB format | ![]() | 251.5 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 353.4 KB | Display | ![]() |
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Full document | ![]() | 530.4 KB | Display | |
Data in XML | ![]() | 17.4 KB | Display | |
Data in CIF | ![]() | 28.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 5666.237 Da / Num. of mol.: 1 / Fragment: WWIII DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1725.894 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Description: AN IDENTICAL PEPTIDE WAS MADE SYNTHETICALLY USING STANDARD F-MOC CHEMISTRY FOR NMR SAMPLES REQUIRING UNLABELED BP2 PEPTIDE. Plasmid: PGEX4T2 / Species (production host): Escherichia coli / Production host: ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample conditions | Ionic strength: 0.01 / pH: 6.5 / Pressure: 1 atm / Temperature: 303 K | |||||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: Preliminary structures were calculated using CNS1.0. These structures were then used as input into the program ARIA1.0 for noe assignment and structure refinement. These structures were ...Details: Preliminary structures were calculated using CNS1.0. These structures were then used as input into the program ARIA1.0 for noe assignment and structure refinement. These structures were calculated using 1799 unambiguous and 214 ambiguous NOEs, 14 hydrogen bond restraints, 44 dihedral angle restraints and directly refined against 33 Jhnha coupling constants. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 170 / Conformers submitted total number: 15 |