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- PDB-2kz7: Solution structure of the CARMIL CAH3a/b domain bound to capping ... -
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Basic information
Entry | Database: PDB / ID: 2kz7 | ||||||
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Title | Solution structure of the CARMIL CAH3a/b domain bound to capping protein (CP) | ||||||
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![]() | PROTEIN BINDING / TROSY / Paramagnetic relaxation enhancement / protein-protein complex | ||||||
Function / homology | ![]() barbed-end actin filament uncapping / positive regulation of lamellipodium organization / negative regulation of barbed-end actin filament capping / Advanced glycosylation endproduct receptor signaling / RHOD GTPase cycle / RHOF GTPase cycle / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / COPI-independent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / macropinosome ...barbed-end actin filament uncapping / positive regulation of lamellipodium organization / negative regulation of barbed-end actin filament capping / Advanced glycosylation endproduct receptor signaling / RHOD GTPase cycle / RHOF GTPase cycle / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / COPI-independent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / macropinosome / Factors involved in megakaryocyte development and platelet production / actin filament network formation / WASH complex / : / F-actin capping protein complex / macropinocytosis / urate metabolic process / negative regulation of filopodium assembly / regulation of Arp2/3 complex-mediated actin nucleation / Factors involved in megakaryocyte development and platelet production / cell junction assembly / ruffle organization / barbed-end actin filament capping / actin polymerization or depolymerization / regulation of cell morphogenesis / regulation of lamellipodium assembly / intermediate filament cytoskeleton / lamellipodium assembly / establishment or maintenance of cell polarity / cortical cytoskeleton / positive regulation of actin filament polymerization / filamentous actin / brush border / positive regulation of substrate adhesion-dependent cell spreading / positive regulation of stress fiber assembly / cytoskeleton organization / hippocampal mossy fiber to CA3 synapse / Schaffer collateral - CA1 synapse / cell morphogenesis / Z disc / actin filament binding / cell migration / lamellipodium / actin cytoskeleton organization / postsynaptic density / positive regulation of cell migration / nuclear speck / protein-containing complex binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics, simulated annealing, torsion angle dynamics | ||||||
![]() | Zwolak, A. / Tjandra, N. | ||||||
![]() | ![]() Title: Solution structure of the CARMIL CAH3a/b domain bound to capping protein (CP) Authors: Zwolak, A. / Uruno, T. / Piszczek, G.P. / Hammer III, J.A. / Tjandra, N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.9 MB | Display | ![]() |
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PDB format | ![]() | 1.6 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 381.6 KB | Display | ![]() |
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Full document | ![]() | 581.7 KB | Display | |
Data in XML | ![]() | 140.4 KB | Display | |
Data in CIF | ![]() | 202.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar 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: 33001.789 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | Mass: 31403.449 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Protein | Mass: 9449.754 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample |
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Sample conditions | Ionic strength: 100 / pH: 6.5 / Pressure: ambient / Temperature: 305 K |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: molecular dynamics, simulated annealing, torsion angle dynamics Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 10 |