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- PDB-2k0f: Calmodulin complexed with calmodulin-binding peptide from smooth ... -
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Basic information
Entry | Database: PDB / ID: 2k0f | ||||||
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Title | Calmodulin complexed with calmodulin-binding peptide from smooth muscle myosin light chain kinase | ||||||
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![]() | METAL BINDING PROTEIN / EF HANDS / ENSEMBLE / HELIX BUNDLE / CALCIUM BINDING | ||||||
Function / homology | ![]() aorta smooth muscle tissue morphogenesis / tonic smooth muscle contraction / myosin-light-chain kinase / myosin light chain kinase activity / muscle structure development / cellular hypotonic response / : / bleb assembly / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding ...aorta smooth muscle tissue morphogenesis / tonic smooth muscle contraction / myosin-light-chain kinase / myosin light chain kinase activity / muscle structure development / cellular hypotonic response / : / bleb assembly / establishment of protein localization to mitochondrial membrane / type 3 metabotropic glutamate receptor binding / positive regulation of calcium ion transport / CaM pathway / Cam-PDE 1 activation / Sodium/Calcium exchangers / regulation of synaptic vesicle endocytosis / Calmodulin induced events / 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 / organelle localization by membrane tethering / negative regulation of calcium ion export across plasma membrane / regulation of synaptic vesicle exocytosis / CLEC7A (Dectin-1) induces NFAT activation / regulation of cardiac muscle cell action potential / mitochondrion-endoplasmic reticulum membrane tethering / autophagosome membrane docking / Activation of RAC1 downstream of NMDARs / response to corticosterone / positive regulation of wound healing / nitric-oxide synthase binding / positive regulation of ryanodine-sensitive calcium-release channel activity / 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 / Phase 0 - rapid depolarisation / protein phosphatase activator activity / RHO GTPases activate PAKs / positive regulation of phosphoprotein phosphatase activity / Ion transport by P-type ATPases / cleavage furrow / Long-term potentiation / Uptake and function of anthrax toxins / Calcineurin activates NFAT / Regulation of MECP2 expression and activity / adenylate cyclase binding / catalytic complex / DARPP-32 events / detection of calcium ion / smooth muscle contraction / regulation of cardiac muscle contraction / negative regulation of ryanodine-sensitive calcium-release channel activity / Smooth Muscle Contraction / RHO GTPases activate IQGAPs / calcium channel inhibitor activity / cellular response to interferon-beta / positive regulation of DNA binding / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / Protein methylation / phosphatidylinositol 3-kinase binding / eNOS activation / Activation of AMPK downstream of NMDARs / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / enzyme regulator activity / stress fiber / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / positive regulation of protein dephosphorylation / Ion homeostasis / regulation of calcium-mediated signaling / regulation of ryanodine-sensitive calcium-release channel activity / titin binding / positive regulation of protein autophosphorylation / voltage-gated potassium channel complex / sperm midpiece / calcium channel complex / response to amphetamine / activation of adenylate cyclase activity / substantia nigra development / adenylate cyclase activator activity / Ras activation upon Ca2+ influx through NMDA receptor / nitric-oxide synthase regulator activity / regulation of heart rate / sarcomere / protein serine/threonine kinase activator activity / FCERI mediated Ca+2 mobilization / FCGR3A-mediated IL10 synthesis / VEGFR2 mediated vascular permeability / positive regulation of peptidyl-threonine phosphorylation / regulation of cytokinesis / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / VEGFR2 mediated cell proliferation / positive regulation of nitric-oxide synthase activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / CHARMM | ||||||
Model details | STRUCTURAL ENSEMBLE OF CALMODULIN COMPLEXED WITH CALMODULIN-BINDING PEPTIDE FROM SMOOTH MUSCLE ...STRUCTURAL ENSEMBLE OF CALMODULIN COMPLEXED WITH CALMODULIN-BINDING PEPTIDE FROM SMOOTH MUSCLE MYOSIN LIGHT CHAIN KINASE DETERMINED WITH MUMO | ||||||
![]() | Gsponer, J. / Christodoulou, J. / Cavalli, A. / Bui, J.M. / Richter, B. / Dobson, C.M. / Vendruscolo, M. | ||||||
![]() | ![]() Title: A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction Authors: Gsponer, J. / Christodoulou, J. / Cavalli, A. / Bui, J.M. / Richter, B. / Dobson, C.M. / Vendruscolo, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 7.5 MB | Display | ![]() |
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PDB format | ![]() | 6.3 MB | Display | ![]() |
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-Validation report
Summary document | ![]() | 369.1 KB | Display | ![]() |
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Full document | ![]() | 2.3 MB | Display | |
Data in XML | ![]() | 518.7 KB | Display | |
Data in CIF | ![]() | 669.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 16721.350 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 2214.601 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: sequence occurs naturally in humans / References: UniProt: Q15746, UniProt: P11799*PLUS |
#3: Chemical | ChemComp-CA / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: STRUCTURAL ENSEMBLE OF CALMODULIN COMPLEXED WITH CALMODULIN-BINDING PEPTIDE FROM SMOOTH MUSCLE MYOSIN LIGHT CHAIN KINASE DETERMINED WITH MUMO |
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Sample preparation
Sample conditions | Pressure units: atm / Temperature units: K |
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-NMR measurement
NMR spectrometer | Type: NULL NULL |
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Processing
NMR software | Name: CHARMM / Version: C30 Developer: B.R.BROOKS, R.E.BRUCCOLERI, B.D.OLAFSON,D.J.STATES, S.SWAMINATHAN, M.KARLPLUS Classification: refinement |
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Refinement | Method: CHARMM / Software ordinal: 1 Details: PROGRAM : CHARMM C30 AUTHORS : B.R.BROOKS, R.E.BRUCCOLERI, B.D.OLAFSON,D.J.STATES, S.SWAMINATHAN, M.KARLPLUS |
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 160 / Conformers submitted total number: 160 |