+
Open data
-
Basic information
Entry | Database: PDB / ID: 2mtp | ||||||
---|---|---|---|---|---|---|---|
Title | The structure of Filamin repeat 21 bound to integrin | ||||||
![]() |
| ||||||
![]() | PROTEIN BINDING/Cell Adhesion / integrin / filamin / PROTEIN BINDING-Cell Adhesion complex | ||||||
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 / adenylate cyclase-inhibiting dopamine receptor signaling pathway / formation of radial glial scaffolds / positive regulation of integrin-mediated signaling pathway / actin crosslink formation / tubulin deacetylation ...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 / adenylate cyclase-inhibiting dopamine receptor signaling pathway / formation of radial glial scaffolds / positive regulation of integrin-mediated signaling pathway / actin crosslink formation / tubulin deacetylation / blood coagulation, intrinsic pathway / protein localization to bicellular tight junction / OAS antiviral response / tube development / : / regulation of serotonin uptake / positive regulation of adenylate cyclase-inhibiting opioid receptor signaling pathway / alpha9-beta1 integrin-ADAM8 complex / regulation of trophoblast cell migration / integrin alphaIIb-beta3 complex / positive regulation of actin filament bundle assembly / regulation of postsynaptic neurotransmitter receptor diffusion trapping / maintenance of postsynaptic specialization structure / alphav-beta3 integrin-vitronectin complex / positive regulation of neuron migration / regulation of extracellular matrix organization / positive regulation of glomerular mesangial cell proliferation / platelet alpha granule membrane / integrin alphav-beta3 complex / negative regulation of lipoprotein metabolic process / Cell-extracellular matrix interactions / alphav-beta3 integrin-PKCalpha complex / fibrinogen binding / Fc-gamma receptor I complex binding / blood coagulation, fibrin clot formation / alphav-beta3 integrin-HMGB1 complex / vascular endothelial growth factor receptor 2 binding / negative regulation of lipid transport / positive regulation of potassium ion transmembrane transport / apical dendrite / positive regulation of vascular endothelial growth factor signaling pathway / positive regulation of neural precursor cell proliferation / regulation of release of sequestered calcium ion into cytosol / Elastic fibre formation / positive regulation of platelet activation / glycinergic synapse / mesodermal cell differentiation / cell-substrate junction assembly / alphav-beta3 integrin-IGF-1-IGF1R complex / platelet-derived growth factor receptor binding / filopodium membrane / extracellular matrix binding / angiogenesis involved in wound healing / positive regulation of vascular endothelial growth factor receptor signaling pathway / regulation of bone resorption / apolipoprotein A-I-mediated signaling pathway / positive regulation of cell adhesion mediated by integrin / positive regulation of leukocyte migration / protein localization to cell surface / apoptotic cell clearance / wound healing, spreading of cells / integrin complex / wound healing, spreading of epidermal cells / heterotypic cell-cell adhesion / positive regulation of fibroblast migration / podosome / positive regulation of smooth muscle cell migration / negative regulation of transcription by RNA polymerase I / smooth muscle cell migration / Molecules associated with elastic fibres / megakaryocyte development / Mechanical load activates signaling by PIEZO1 and integrins in osteocytes / positive regulation of cell-matrix adhesion / negative chemotaxis / cellular response to insulin-like growth factor stimulus / cell adhesion mediated by integrin / GP1b-IX-V activation signalling / Syndecan interactions / p130Cas linkage to MAPK signaling for integrins / positive regulation of osteoblast proliferation / microvillus membrane / regulation of postsynaptic neurotransmitter receptor internalization / protein disulfide isomerase activity / receptor clustering / cortical cytoskeleton / SMAD binding / cell-substrate adhesion / platelet-derived growth factor receptor signaling pathway / RHO GTPases activate PAKs / PECAM1 interactions / TGF-beta receptor signaling activates SMADs / GRB2:SOS provides linkage to MAPK signaling for Integrins / semaphorin-plexin signaling pathway / lamellipodium membrane / fibronectin binding / positive regulation of bone resorption / negative regulation of macrophage derived foam cell differentiation / negative regulation of lipid storage / cilium assembly / mitotic spindle assembly Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Liu, J. / Qin, J. | ||||||
![]() | ![]() Title: Structural mechanism of integrin inactivation by filamin. Authors: Liu, J. / Das, M. / Yang, J. / Ithychanda, S.S. / Yakubenko, V.P. / Plow, E.F. / Qin, J. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 899.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 655.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 152.2 KB | Display | |
Data in CIF | ![]() | 179.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 9762.721 Da / Num. of mol.: 1 / Fragment: UNP residues 2236-2330 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Protein/peptide | Mass: 2581.789 Da / Num. of mol.: 1 / Fragment: UNP residues 1019-1039 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Protein/peptide | Mass: 5618.318 Da / Num. of mol.: 1 / Fragment: UNP residues 742-788 / Mutation: L717K, L718K Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details | Contents: 1 mM [U-100% 13C; U-100% 15N; U-80% 2H] protein, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample | Conc.: 1 mM / Component: entity_1-1 / Isotopic labeling: [U-100% 13C; U-100% 15N; U-80% 2H] |
Sample conditions | Ionic strength: 25 / pH: 6.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
|
---|
-
Processing
NMR software |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||
NMR representative | Selection criteria: lowest energy | |||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |