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- PDB-3g9w: Crystal Structure of Talin2 F2-F3 in Complex with the Integrin Be... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3g9w | ||||||
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Title | Crystal Structure of Talin2 F2-F3 in Complex with the Integrin Beta1D Cytoplasmic Tail | ||||||
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![]() | CELL ADHESION / protein-protein complex / PH domain superfold / PTB domain / helical bundle / intrinsically unstructured | ||||||
Function / homology | ![]() integrin alpha8-beta1 complex / myoblast fate specification / integrin alpha3-beta1 complex / integrin alpha5-beta1 complex / integrin alpha7-beta1 complex / integrin alpha10-beta1 complex / integrin alpha11-beta1 complex / positive regulation of glutamate uptake involved in transmission of nerve impulse / regulation of inward rectifier potassium channel activity / regulation of collagen catabolic process ...integrin alpha8-beta1 complex / myoblast fate specification / integrin alpha3-beta1 complex / integrin alpha5-beta1 complex / integrin alpha7-beta1 complex / integrin alpha10-beta1 complex / integrin alpha11-beta1 complex / positive regulation of glutamate uptake involved in transmission of nerve impulse / regulation of inward rectifier potassium channel activity / regulation of collagen catabolic process / integrin alpha9-beta1 complex / integrin alpha4-beta1 complex / cardiac cell fate specification / integrin binding involved in cell-matrix adhesion / cell-cell adhesion mediated by integrin / C-X3-C chemokine binding / integrin alpha1-beta1 complex / regulation of synapse pruning / collagen binding involved in cell-matrix adhesion / integrin alpha2-beta1 complex / Localization of the PINCH-ILK-PARVIN complex to focal adhesions / reactive gliosis / cerebellar climbing fiber to Purkinje cell synapse / formation of radial glial scaffolds / Other semaphorin interactions / Formation of the ureteric bud / CD40 signaling pathway / positive regulation of vascular endothelial growth factor signaling pathway / integrin alphav-beta1 complex / calcium-independent cell-matrix adhesion / positive regulation of fibroblast growth factor receptor signaling pathway / Fibronectin matrix formation / basement membrane organization / myelin sheath abaxonal region / CHL1 interactions / cardiac muscle cell myoblast differentiation / Laminin interactions / MET interacts with TNS proteins / germ cell migration / fascia adherens / leukocyte tethering or rolling / cardiac muscle cell differentiation / cell projection organization / Platelet Adhesion to exposed collagen / myoblast fusion / Elastic fibre formation / mesodermal cell differentiation / axon extension / positive regulation of fibroblast migration / cell migration involved in sprouting angiogenesis / wound healing, spreading of epidermal cells / regulation of spontaneous synaptic transmission / myoblast differentiation / heterotypic cell-cell adhesion / integrin complex / dendrite morphogenesis / Basigin interactions / Molecules associated with elastic fibres / muscle organ development / negative regulation of Rho protein signal transduction / lamellipodium assembly / MET activates PTK2 signaling / negative regulation of vasoconstriction / cell adhesion mediated by integrin / Syndecan interactions / leukocyte cell-cell adhesion / positive regulation of wound healing / maintenance of blood-brain barrier / positive regulation of neuroblast proliferation / sarcomere organization / cell-substrate adhesion / homophilic cell adhesion via plasma membrane adhesion molecules / TGF-beta receptor signaling activates SMADs / establishment of mitotic spindle orientation / cleavage furrow / glial cell projection / cellular response to low-density lipoprotein particle stimulus / fibronectin binding / negative regulation of anoikis / intercalated disc / RHOG GTPase cycle / negative regulation of neuron differentiation / ECM proteoglycans / neuroblast proliferation / RAC2 GTPase cycle / RAC3 GTPase cycle / Integrin cell surface interactions / cellular defense response / coreceptor activity / phagocytosis / laminin binding / cell adhesion molecule binding / ruffle / RAC1 GTPase cycle / B cell differentiation / protein tyrosine kinase binding / cell-matrix adhesion / positive regulation of GTPase activity / synaptic membrane / Signal transduction by L1 Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Anthis, N.J. / Wegener, K.L. / Ye, F. / Kim, C. / Lowe, E.D. / Vakonakis, I. / Bate, N. / Critchley, D.R. / Ginsberg, M.H. / Campbell, I.D. | ||||||
![]() | ![]() Title: The structure of an integrin/talin complex reveals the basis of inside-out signal transduction Authors: Anthis, N.J. / Wegener, K.L. / Ye, F. / Kim, C. / Goult, B.T. / Lowe, E.D. / Vakonakis, I. / Bate, N. / Critchley, D.R. / Ginsberg, M.H. / Campbell, I.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 226.9 KB | Display | ![]() |
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PDB format | ![]() | 182.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 482.4 KB | Display | ![]() |
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Full document | ![]() | 489.1 KB | Display | |
Data in XML | ![]() | 25.4 KB | Display | |
Data in CIF | ![]() | 35.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1mixS ![]() 1mk7S ![]() 1mk9S S: Starting model for refinement |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 25762.516 Da / Num. of mol.: 2 / Fragment: F2-F3 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 6190.161 Da / Num. of mol.: 2 / Fragment: Cytoplasmic Tail Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-GOL / #4: Chemical | #5: Water | ChemComp-HOH / | Sequence details | THE SEQUENCE OF CHAIN C, D IS ISOFORM BETA-1D AS LISTED IN UNP ENTRY, P05556-5 | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 58.82 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 0.1M ammonium acetate, 0.02M magnesium chloride, 0.05M HEPES, 5% PEG 8k, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Jun 26, 2008 Details: Monochromator (horizontally side diffracting Silicon 111 crystal) |
Radiation | Monochromator: horizontally diffracting monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8726 Å / Relative weight: 1 |
Reflection | Resolution: 2.165→41.95 Å / Num. all: 41528 / Num. obs: 41362 / % possible obs: 99.6 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.7 % / Biso Wilson estimate: 25.312 Å2 / Rmerge(I) obs: 0.114 / Rsym value: 0.114 / Net I/σ(I): 8.3 |
Reflection shell | Resolution: 2.165→2.28 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.338 / Mean I/σ(I) obs: 3.5 / Num. unique all: 5982 / Rsym value: 0.338 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entries 1MIX, 1MK7, 1MK9 Resolution: 2.165→41.941 Å / SU ML: 0.32 / σ(F): 0.97 / Stereochemistry target values: Engh & Huber
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 36.249 Å2 / ksol: 0.325 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.26 Å2
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Refinement step | Cycle: LAST / Resolution: 2.165→41.941 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 28
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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