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- PDB-2vil: REFINED STRUCTURE OF THE ACTIN-SEVERING DOMAIN VILLIN 14T, DETERM... -
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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 | |||||||||
![]() | VILLIN 14T | |||||||||
![]() | ACTIN-BINDING PROTEIN / CAPPING PROTEIN / CALCIUM-BINDING PROTEIN / CYTOSKELETAL PROTEIN | |||||||||
Function / homology | ![]() 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 / barbed-end actin filament capping / actin polymerization or depolymerization / 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 / response to bacterium / epidermal growth factor receptor signaling pathway / 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 | ![]() ![]() | |||||||||
Method | SOLUTION NMR / distance geometry | |||||||||
![]() | Markus, M.A. / Matsudaira, P. / Wagner, G. | |||||||||
![]() | ![]() Title: Refined structure of villin 14T and a detailed comparison with other actin-severing domains. Authors: Markus, M.A. / Matsudaira, P. / Wagner, G. #1: ![]() 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: ![]() Title: Solution Structure of Villin 14T, a Domain Conserved Among Actin-Severing Proteins Authors: Markus, M.A. / Nakayama, T. / Matsudaira, P. / Wagner, G. #3: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 432.7 KB | Display | ![]() |
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PDB format | ![]() | 355.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 345.5 KB | Display | ![]() |
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Full document | ![]() | 521.4 KB | Display | |
Data in XML | ![]() | 56.4 KB | Display | |
Data in CIF | ![]() | 75.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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 | Mass: 14174.928 Da / Num. of mol.: 1 / Fragment: RESIDUES 1 - 126 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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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
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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 |