[English] 日本語
![](img/lk-miru.gif)
- PDB-3isw: Crystal structure of filamin-A immunoglobulin-like repeat 21 boun... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 3isw | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of filamin-A immunoglobulin-like repeat 21 bound to an N-terminal peptide of CFTR | ||||||
![]() |
| ||||||
![]() | STRUCTURAL PROTEIN / protein-peptide complex / Acetylation / Actin-binding / Alternative splicing / Cytoplasm / Cytoskeleton / Disease mutation / Phosphoprotein / Polymorphism / ATP-binding / Chloride / Chloride channel / Glycoprotein / Hydrolase / Ion transport / Ionic channel / Membrane / Nucleotide-binding / Transmembrane / Transport | ||||||
Function / homology | ![]() regulation of membrane repolarization during atrial cardiac muscle cell action potential / regulation of membrane repolarization during cardiac muscle cell action potential / establishment of Sertoli cell barrier / Myb complex / glycoprotein Ib-IX-V complex / formation of radial glial scaffolds / adenylate cyclase-inhibiting dopamine receptor signaling pathway / positive regulation of voltage-gated chloride channel activity / positive regulation of cyclic nucleotide-gated ion channel activity / positive regulation of integrin-mediated signaling pathway ...regulation of membrane repolarization during atrial cardiac muscle cell action potential / regulation of membrane repolarization during cardiac muscle cell action potential / establishment of Sertoli cell barrier / Myb complex / glycoprotein Ib-IX-V complex / formation of radial glial scaffolds / adenylate cyclase-inhibiting dopamine receptor signaling pathway / positive regulation of voltage-gated chloride channel activity / positive regulation of cyclic nucleotide-gated ion channel activity / positive regulation of integrin-mediated signaling pathway / Sec61 translocon complex binding / channel-conductance-controlling ATPase / intracellularly ATP-gated chloride channel activity / positive regulation of enamel mineralization / transepithelial water transport / tubulin deacetylation / cytoplasmic sequestering of protein / RHO GTPases regulate CFTR trafficking / intracellular pH elevation / actin crosslink formation / blood coagulation, intrinsic pathway / amelogenesis / protein localization to bicellular tight junction / chloride channel inhibitor activity / OAS antiviral response / ATPase-coupled inorganic anion transmembrane transporter activity / positive regulation of actin filament bundle assembly / Golgi-associated vesicle membrane / positive regulation of neuron migration / positive regulation of potassium ion transmembrane transport / Cell-extracellular matrix interactions / multicellular organismal-level water homeostasis / early endosome to late endosome transport / apical dendrite / Fc-gamma receptor I complex binding / cell-cell junction organization / cholesterol transport / membrane hyperpolarization / positive regulation of neural precursor cell proliferation / positive regulation of platelet activation / vesicle docking involved in exocytosis / bicarbonate transport / bicarbonate transmembrane transporter activity / chloride channel regulator activity / protein localization to cell surface / wound healing, spreading of cells / chloride transmembrane transporter activity / negative regulation of transcription by RNA polymerase I / sperm capacitation / megakaryocyte development / GP1b-IX-V activation signalling / chloride channel activity / cortical cytoskeleton / positive regulation of axon regeneration / receptor clustering / cholesterol biosynthetic process / RHOQ GTPase cycle / SMAD binding / positive regulation of exocytosis / actin filament bundle / RHO GTPases activate PAKs / positive regulation of insulin secretion involved in cellular response to glucose stimulus / brush border / chloride channel complex / semaphorin-plexin signaling pathway / mitotic spindle assembly / cilium assembly / ATPase-coupled transmembrane transporter activity / potassium channel regulator activity / epithelial to mesenchymal transition / blood vessel remodeling / ABC-type transporter activity / axonal growth cone / heart morphogenesis / positive regulation of substrate adhesion-dependent cell spreading / cellular response to cAMP / release of sequestered calcium ion into cytosol / cellular response to forskolin / chloride transmembrane transport / regulation of cell migration / response to endoplasmic reticulum stress / isomerase activity / dendritic shaft / protein localization to plasma membrane / establishment of localization in cell / G protein-coupled receptor binding / PDZ domain binding / actin filament / protein kinase C binding / Defective CFTR causes cystic fibrosis / synapse organization / Late endosomal microautophagy / clathrin-coated endocytic vesicle membrane / mRNA transcription by RNA polymerase II / trans-Golgi network / establishment of protein localization / ABC-family proteins mediated transport / negative regulation of protein catabolic process / negative regulation of DNA-binding transcription factor activity / recycling endosome Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Xu, Z. / Page, R. / Qin, J. / Ithychanda, S.S. / Liu, J.M. / Misra, S. | ||||||
![]() | ![]() Title: Biochemical basis of the interaction between cystic fibrosis transmembrane conductance regulator and immunoglobulin-like repeats of filamin. Authors: Smith, L. / Page, R.C. / Xu, Z. / Kohli, E. / Litman, P. / Nix, J.C. / Ithychanda, S.S. / Liu, J. / Qin, J. / Misra, S. / Liedtke, C.M. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 51.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 36.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 2brqS S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Details | THE BIOLOGICAL ASSEMBLY IS THE DIMERIC COMPLEX OF THE PROTEIN WITH THE PEPTIDE, REPRESENTED BY THE ENTIRE CONTENTS OF THE ASYMMETRIC UNIT. THE SOFTWARE-GENERATED WORD 'TRIMERIC' IN REMARK 350 IS A POLYMERIC COUNT. |
-
Components
#1: Protein | Mass: 10177.196 Da / Num. of mol.: 2 / Fragment: UNP residues 2236-2329 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | | Mass: 2009.345 Da / Num. of mol.: 1 / Fragment: UNP residues 5-22 / Mutation: R21A / Source method: obtained synthetically Details: Synthetic peptide based on the sequence 5-22 of Homo sapiens CFTR (UniProt entry P13569, CFTR_HUMAN) References: UniProt: P13569 #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 5.13 Å3/Da / Density % sol: 76.02 % |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 0.1M Bis-Tris Propane pH 7.0, 60% Tacsimate, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: NOIR-1 / Detector: CCD / Date: Jul 1, 2007 Details: ROSENBAUM-ROCK MONOCHROMATOR FOR SAGITAL FOCUSING, ROSENBAUM-ROCK VERTICAL FOCUSING MIRROR |
Radiation | Monochromator: double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→42.97 Å / Num. all: 13108 / Num. obs: 12452 / % possible obs: 96.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 5 / Redundancy: 8.53 % / Biso Wilson estimate: 75.7 Å2 / Rmerge(I) obs: 0.071 / Rsym value: 0.071 / Χ2: 0.94 / Net I/σ(I): 13.8 / Scaling rejects: 3169 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 10.41 % / Rmerge(I) obs: 0.472 / Mean I/σ(I) obs: 3.3 / Num. unique all: 1177 / Rsym value: 0.472 / Χ2: 1.34 / % possible all: 98.5 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB entry 2BRQ Resolution: 2.8→34.73 Å / Cor.coef. Fo:Fc: 0.919 / Cor.coef. Fo:Fc free: 0.907 / Occupancy max: 1 / Occupancy min: 1 / SU B: 14.066 / SU ML: 0.277 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.403 / ESU R Free: 0.313 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 104.74 Å2 / Biso mean: 69.191 Å2 / Biso min: 37.96 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→34.73 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.8→2.873 Å / Total num. of bins used: 20
|