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- PDB-1unc: Solution structure of the human villin C-terminal headpiece subdomain -

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Basic information

Entry
Database: PDB / ID: 1unc
TitleSolution structure of the human villin C-terminal headpiece subdomain
ComponentsVILLIN 1
KeywordsACTIN BINDING / F-ACTIN BINDING / CYTOSKELETON / HEADPIECE SUBDOMAIN
Function / homology
Function and homology information


terminal web assembly / intestinal D-glucose absorption / regulation of microvillus length / regulation of actin nucleation / cytoplasmic actin-based contraction involved in cell motility / positive regulation of actin filament depolymerization / lysophosphatidic acid binding / regulation of lamellipodium morphogenesis / filopodium tip / positive regulation of lamellipodium morphogenesis ...terminal web assembly / intestinal D-glucose absorption / regulation of microvillus length / regulation of actin nucleation / cytoplasmic actin-based contraction involved in cell motility / positive regulation of actin filament depolymerization / lysophosphatidic acid binding / regulation of lamellipodium morphogenesis / filopodium tip / positive regulation of lamellipodium morphogenesis / positive regulation of actin filament bundle assembly / actin filament severing / regulation of wound healing / actin filament capping / actin filament depolymerization / positive regulation of multicellular organism growth / 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 / brush border / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / microvillus / cellular response to epidermal growth factor stimulus / ruffle / epithelial cell differentiation / phosphatidylinositol-4,5-bisphosphate binding / actin filament polymerization / filopodium / positive regulation of protein localization to plasma membrane / response to bacterium / epidermal growth factor receptor signaling pathway / actin filament binding / actin cytoskeleton / lamellipodium / regulation of cell shape / protein-containing complex assembly / positive regulation of cell migration / apoptotic process / calcium ion binding / protein homodimerization activity / extracellular exosome / identical protein binding / plasma membrane / cytoplasm
Similarity search - Function
Villin headpiece / Villin headpiece domain superfamily / Villin headpiece domain / Headpiece (HP) domain profile. / Villin headpiece domain / Gelsolin-like domain superfamily / Villin/Gelsolin / Gelsolin homology domain / Gelsolin-like domain / Gelsolin repeat / ADF-H/Gelsolin-like domain superfamily
Similarity search - Domain/homology
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsVermeulen, W. / Van Troys, M. / Vanhaesebrouck, P. / Verschueren, M. / Fant, F. / Ampe, C. / Martins, J. / Borremans, F.
CitationJournal: Protein Sci. / Year: 2004
Title: Solution Structures of the C-Terminal Headpiece Subdomains of Human Villin and Advillin, Evaluation of Headpiece F-Actin-Binding Requirements
Authors: Vermeulen, W. / Vanhaesebrouck, P. / Van Troys, M. / Verschueren, M. / Fant, F. / Goethals, M. / Ampe, C. / Martins, J. / Borremans, F.
History
DepositionSep 9, 2003Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 15, 2004Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: VILLIN 1


Theoretical massNumber of molelcules
Total (without water)4,0311
Polymers4,0311
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)25 / 500target function
Representative

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Components

#1: Protein/peptide VILLIN 1 / VILLIN


Mass: 4030.668 Da / Num. of mol.: 1 / Fragment: HEADPIECE SUBDOMAIN, RESIDUES 792-826 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P09327

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131DQF-COSY
141E.COSY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING 2D-1H NMR

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Sample preparation

Sample conditionspH: 4.3 / Pressure: 1 atm / Temperature: 294 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 500 MHz

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Processing

NMR software
NameDeveloperClassification
INSIGHT2ACCELRYSrefinement
DYANAstructure solution
RefinementMethod: torsion angle dynamics / Software ordinal: 1
Details: AMBER FORCEFIELD REFINEMENT USING SIMULATED ANNEALING
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 500 / Conformers submitted total number: 25

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