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- PDB-2r28: The complex Structure of Calmodulin Bound to a Calcineurin Peptide -
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Basic information
Entry | Database: PDB / ID: 2r28 | ||||||
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Title | The complex Structure of Calmodulin Bound to a Calcineurin Peptide | ||||||
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![]() | METAL BINDING PROTEIN/Hydrolase / Protein-peptide complex / Acetylation / Calcium / Methylation / Phosphorylation / Ubl conjugation / Alternative splicing / Calmodulin-binding / Hydrolase / Iron / Metal-binding / Nucleus / Protein phosphatase / Zinc / METAL BINDING PROTEIN-Hydrolase COMPLEX | ||||||
Function / homology | ![]() negative regulation of angiotensin-activated signaling pathway / regulation of cell proliferation involved in kidney morphogenesis / positive regulation of glomerulus development / negative regulation of calcium ion import across plasma membrane / negative regulation of signaling / positive regulation of saliva secretion / positive regulation of cardiac muscle hypertrophy in response to stress / positive regulation of calcium ion import across plasma membrane / calmodulin-dependent protein phosphatase activity / calcineurin complex ...negative regulation of angiotensin-activated signaling pathway / regulation of cell proliferation involved in kidney morphogenesis / positive regulation of glomerulus development / negative regulation of calcium ion import across plasma membrane / negative regulation of signaling / positive regulation of saliva secretion / positive regulation of cardiac muscle hypertrophy in response to stress / positive regulation of calcium ion import across plasma membrane / calmodulin-dependent protein phosphatase activity / calcineurin complex / positive regulation of connective tissue replacement / negative regulation of dendrite morphogenesis / calcineurin-mediated signaling / slit diaphragm / protein serine/threonine phosphatase complex / peptidyl-serine dephosphorylation / renal filtration / calcineurin-NFAT signaling cascade / skeletal muscle tissue regeneration / : / transition between fast and slow fiber / positive regulation of calcineurin-NFAT signaling cascade / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / cardiac muscle hypertrophy in response to stress / positive regulation of osteoclast differentiation / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / dendrite morphogenesis / Calmodulin induced events / regulation of synaptic vesicle endocytosis / Reduction of cytosolic Ca++ levels / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Activation of Ca-permeable Kainate Receptor / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / PKA activation / negative regulation of high voltage-gated calcium channel activity / CaMK IV-mediated phosphorylation of CREB / Glycogen breakdown (glycogenolysis) / positive regulation of cyclic-nucleotide phosphodiesterase activity / regulation of synaptic vesicle exocytosis / organelle localization by membrane tethering / negative regulation of calcium ion export across plasma membrane / CLEC7A (Dectin-1) induces NFAT activation / cyclosporin A binding / myosin phosphatase activity / extrinsic component of plasma membrane / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / regulation of cardiac muscle cell action potential / Activation of RAC1 downstream of NMDARs / response to corticosterone / protein serine/threonine phosphatase activity / postsynaptic modulation of chemical synaptic transmission / positive regulation of DNA binding / protein-serine/threonine phosphatase / positive regulation of ryanodine-sensitive calcium-release channel activity / nitric-oxide synthase binding / regulation of cell communication by electrical coupling involved in cardiac conduction / Negative regulation of NMDA receptor-mediated neuronal transmission / negative regulation of peptidyl-threonine phosphorylation / Synthesis of IP3 and IP4 in the cytosol / Unblocking of NMDA receptors, glutamate binding and activation / positive regulation of activated T cell proliferation / dephosphorylation / Phase 0 - rapid depolarisation / negative regulation of ryanodine-sensitive calcium-release channel activity / protein phosphatase activator activity / RHO GTPases activate PAKs / positive regulation of endocytosis / : / Ion transport by P-type ATPases / Long-term potentiation / Uptake and function of anthrax toxins / Regulation of MECP2 expression and activity / Calcineurin activates NFAT / adenylate cyclase binding / catalytic complex / positive regulation of cell adhesion / DARPP-32 events / detection of calcium ion / regulation of cardiac muscle contraction / regulation of ryanodine-sensitive calcium-release channel activity / Smooth Muscle Contraction / epidermis development / cellular response to interferon-beta / RHO GTPases activate IQGAPs / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / calcium channel inhibitor activity / negative regulation of insulin secretion / positive regulation of osteoblast differentiation / multicellular organismal response to stress / Protein methylation / phosphatidylinositol 3-kinase binding / eNOS activation / skeletal muscle fiber development / enzyme regulator activity / activation of adenylate cyclase activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ye, Q. / Zheng, J. / Jia, Z. | ||||||
![]() | ![]() Title: The complex structure of calmodulin bound to a calcineurin peptide. Authors: Ye, Q. / Wang, H. / Zheng, J. / Wei, Q. / Jia, Z. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 84.2 KB | Display | ![]() |
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PDB format | ![]() | 62.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2f2oS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 16852.545 Da / Num. of mol.: 2 / Fragment: Calmodulin-binding domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 2805.458 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q08209, protein-serine/threonine phosphatase #3: Chemical | ChemComp-CA / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.21 Å3/Da / Density % sol: 44.35 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: 20% PEG 3350, 0.2M ammonium phosphate, 0.1M citrite acid , pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 1 / Detector: CCD / Date: Oct 2, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9124 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→66.67 Å / Num. all: 29453 / Num. obs: 28898 / % possible obs: 98.1 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.069 / Rsym value: 0.06 / Net I/σ(I): 9 |
Reflection shell | Resolution: 1.85→1.91 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.759 / Mean I/σ(I) obs: 8.1 / Num. unique all: 2632 / Rsym value: 0.873 / % possible all: 98.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 2F2O Resolution: 1.86→66.67 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0
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Refinement step | Cycle: LAST / Resolution: 1.86→66.67 Å
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LS refinement shell | Resolution: 1.86→1.91 Å / Rfactor Rfree error: 0.17
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