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- PDB-2zpy: Crystal structure of the mouse radxin FERM domain complexed with ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2zpy | ||||||
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Title | Crystal structure of the mouse radxin FERM domain complexed with the mouse CD44 cytoplasmic peptide | ||||||
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![]() | CELL ADHESION / FERM domain / CD44 / Actin capping / Actin-binding / Cell membrane / Cytoplasm / Cytoskeleton / Membrane / Phosphoprotein / Structural protein / Alternative splicing / Glycoprotein / Proteoglycan / Pyrrolidone carboxylic acid / Receptor / Sulfation / Transmembrane | ||||||
Function / homology | ![]() stereocilium base / regulation of organelle assembly / establishment of protein localization to plasma membrane / Hyaluronan uptake and degradation / microvillus assembly / positive regulation of early endosome to late endosome transport / hyaluronic acid binding / macrophage fusion / macrophage migration inhibitory factor receptor complex / regulation of Rap protein signal transduction ...stereocilium base / regulation of organelle assembly / establishment of protein localization to plasma membrane / Hyaluronan uptake and degradation / microvillus assembly / positive regulation of early endosome to late endosome transport / hyaluronic acid binding / macrophage fusion / macrophage migration inhibitory factor receptor complex / regulation of Rap protein signal transduction / negative regulation of regulatory T cell differentiation / Recycling pathway of L1 / Degradation of the extracellular matrix / regulation of lamellipodium morphogenesis / Integrin cell surface interactions / Cell surface interactions at the vascular wall / cell tip / hyaluronan catabolic process / wound healing involved in inflammatory response / positive regulation of adaptive immune response / regulation of postsynaptic neurotransmitter receptor diffusion trapping / positive regulation of protein localization to early endosome / positive regulation of neutrophil apoptotic process / branching involved in prostate gland morphogenesis / type II transforming growth factor beta receptor binding / apical protein localization / stereocilium / negative regulation of mature B cell apoptotic process / negative regulation of CD4-positive, alpha-beta T cell proliferation / channel regulator activity / barbed-end actin filament capping / cellular response to thyroid hormone stimulus / cargo receptor activity / wound healing, spreading of cells / cytokine receptor activity / protein kinase A binding / branching involved in ureteric bud morphogenesis / epidermal growth factor receptor binding / cortical actin cytoskeleton / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / negative regulation of DNA damage response, signal transduction by p53 class mediator / microvillus / cleavage furrow / lamellipodium membrane / positive regulation of G1/S transition of mitotic cell cycle / cell adhesion molecule binding / ruffle / T-tubule / protein kinase A signaling / Neutrophil degranulation / receptor-mediated endocytosis / filopodium / cell projection / regulation of cell growth / phosphoprotein binding / adherens junction / establishment of protein localization / Wnt signaling pathway / negative regulation of inflammatory response / transmembrane signaling receptor activity / neuron projection development / positive regulation of peptidyl-tyrosine phosphorylation / cell migration / lamellipodium / apical part of cell / positive regulation of peptidyl-serine phosphorylation / myelin sheath / actin binding / regulation of cell shape / midbody / basolateral plasma membrane / positive regulation of ERK1 and ERK2 cascade / cell adhesion / inflammatory response / membrane raft / apical plasma membrane / protein domain specific binding / external side of plasma membrane / positive regulation of gene expression / protein kinase binding / cell surface / protein-containing complex / extracellular region / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mori, T. / Kitano, K. / Terawaki, S. / Maesaki, R. / Fukami, Y. / Hakoshima, T. | ||||||
![]() | ![]() Title: Structural basis for CD44 recognition by ERM proteins Authors: Mori, T. / Kitano, K. / Terawaki, S. / Maesaki, R. / Fukami, Y. / Hakoshima, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80.1 KB | Display | ![]() |
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PDB format | ![]() | 58.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 432.3 KB | Display | ![]() |
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Full document | ![]() | 442.5 KB | Display | |
Data in XML | ![]() | 16.1 KB | Display | |
Data in CIF | ![]() | 22.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gc7S S: Starting model for refinement |
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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: 36934.598 Da / Num. of mol.: 1 / Fragment: FERM domain (residues 1-310) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 2177.579 Da / Num. of mol.: 1 / Fragment: residues 293-312 / Source method: obtained synthetically / Details: peptide synthesis / References: UniProt: P15379 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.21 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion / pH: 8.6 Details: 0.1M Tris, 0.2M Potassium thiocyanate, 15% PEG 3350 , pH 8.6, VAPOR DIFFUSION, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Oct 17, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. obs: 21492 / % possible obs: 100 % |
Reflection shell | Resolution: 2.1→2.17 Å / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1GC7 Resolution: 2.1→20 Å
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Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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