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Yorodumi- PDB-2vil: REFINED STRUCTURE OF THE ACTIN-SEVERING DOMAIN VILLIN 14T, DETERM... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2vil | |||||||||
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Title | REFINED STRUCTURE OF THE ACTIN-SEVERING DOMAIN VILLIN 14T, DETERMINED BY SOLUTION NMR, 11 STRUCTURES | |||||||||
Components | VILLIN 14T | |||||||||
Keywords | ACTIN-BINDING PROTEIN / CAPPING PROTEIN / CALCIUM-BINDING PROTEIN / CYTOSKELETAL PROTEIN | |||||||||
Function / homology | Function and homology information regulation of actin nucleation / cytoplasmic actin-based contraction involved in cell motility / lysophosphatidic acid binding / regulation of lamellipodium morphogenesis / filopodium tip / positive regulation of actin filament bundle assembly / actin filament severing / regulation of wound healing / actin filament capping / actin filament depolymerization ...regulation of actin nucleation / cytoplasmic actin-based contraction involved in cell motility / lysophosphatidic acid binding / regulation of lamellipodium morphogenesis / filopodium tip / positive regulation of actin filament bundle assembly / actin filament severing / regulation of wound healing / actin filament capping / actin filament depolymerization / actin polymerization or depolymerization / barbed-end actin filament capping / cellular response to hepatocyte growth factor stimulus / positive regulation of epithelial cell migration / actin filament bundle / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / microvillus / cellular response to epidermal growth factor stimulus / ruffle / phosphatidylinositol-4,5-bisphosphate binding / actin filament polymerization / filopodium / epidermal growth factor receptor signaling pathway / response to bacterium / actin filament binding / actin cytoskeleton / lamellipodium / regulation of cell shape / positive regulation of cell migration / calcium ion binding / protein homodimerization activity / cytoplasm Similarity search - Function | |||||||||
Biological species | Gallus gallus (chicken) | |||||||||
Method | SOLUTION NMR / distance geometry | |||||||||
Authors | Markus, M.A. / Matsudaira, P. / Wagner, G. | |||||||||
Citation | Journal: Protein Sci. / Year: 1997 Title: Refined structure of villin 14T and a detailed comparison with other actin-severing domains. Authors: Markus, M.A. / Matsudaira, P. / Wagner, G. #1: Journal: Biochemistry / Year: 1996 Title: Local Mobility within Villin 14T Probed Via Heteronuclear Relaxation Measurements and a Reduced Spectral Density Mapping Authors: Markus, M.A. / Dayie, K.T. / Matsudaira, P. / Wagner, G. #2: Journal: Protein Sci. / Year: 1994 Title: Solution Structure of Villin 14T, a Domain Conserved Among Actin-Severing Proteins Authors: Markus, M.A. / Nakayama, T. / Matsudaira, P. / Wagner, G. #3: Journal: J.Biomol.NMR / Year: 1994 Title: 1H, 15N, 13C and 13Co Resonance Assignments and Secondary Structure of Villin 14T, a Domain Conserved Among Actin-Severing Proteins Authors: Markus, M.A. / Nakayama, T. / Matsudaira, P. / Wagner, G. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2vil.cif.gz | 432.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2vil.ent.gz | 355.5 KB | Display | PDB format |
PDBx/mmJSON format | 2vil.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2vil_validation.pdf.gz | 345.5 KB | Display | wwPDB validaton report |
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Full document | 2vil_full_validation.pdf.gz | 521.4 KB | Display | |
Data in XML | 2vil_validation.xml.gz | 56.4 KB | Display | |
Data in CIF | 2vil_validation.cif.gz | 75.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vi/2vil ftp://data.pdbj.org/pub/pdb/validation_reports/vi/2vil | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14174.928 Da / Num. of mol.: 1 / Fragment: RESIDUES 1 - 126 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Cell: EPITHELIAL CELLS / Cell line: BL21 / Gene: T7 / Organ: INTESTINE / Plasmid: PAED4, BASED ON T7 PROMOTER / Species (production host): Escherichia coli / Gene (production host): T7 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P02640 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | pH: 4.15 / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
Software |
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NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 | ||||||||||||||||
NMR ensemble | Conformer selection criteria: NOE VIOLATIONS < 0.5 A DIHEDRAL VIOL < 5 DEGREES Conformers calculated total number: 20 / Conformers submitted total number: 11 |