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Open data
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Basic information
Entry | Database: PDB / ID: 2l35 | ||||||
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Title | Structure of the DAP12-NKG2C transmembrane heterotrimer | ||||||
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![]() | PROTEIN BINDING / Immunoreceptor / transmembrane assembly / DAP12-NKG2C complex | ||||||
Function / homology | ![]() myeloid leukocyte activation / stimulatory killer cell immunoglobulin-like receptor signaling pathway / positive regulation of receptor localization to synapse / positive regulation of macrophage fusion / positive regulation of osteoclast development / microglial cell activation involved in immune response / positive regulation of natural killer cell activation / negative regulation of transforming growth factor beta1 production / positive regulation of microglial cell mediated cytotoxicity / Other semaphorin interactions ...myeloid leukocyte activation / stimulatory killer cell immunoglobulin-like receptor signaling pathway / positive regulation of receptor localization to synapse / positive regulation of macrophage fusion / positive regulation of osteoclast development / microglial cell activation involved in immune response / positive regulation of natural killer cell activation / negative regulation of transforming growth factor beta1 production / positive regulation of microglial cell mediated cytotoxicity / Other semaphorin interactions / neutrophil activation involved in immune response / positive regulation of protein localization to cell surface / apoptotic cell clearance / Signal regulatory protein family interactions / negative regulation of type I interferon production / negative regulation of interleukin-10 production / negative regulation of B cell proliferation / stimulatory C-type lectin receptor signaling pathway / negative regulation of long-term synaptic potentiation / response to axon injury / cellular defense response / positive regulation of superoxide anion generation / forebrain development / osteoclast differentiation / secretory granule membrane / DAP12 interactions / positive regulation of interleukin-1 beta production / positive regulation of interleukin-6 production / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / positive regulation of tumor necrosis factor production / DAP12 signaling / actin cytoskeleton organization / molecular adaptor activity / protein stabilization / intracellular signal transduction / signaling receptor binding / Neutrophil degranulation / positive regulation of gene expression / cell surface / signal transduction / protein homodimerization activity / identical protein binding / membrane / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Call, M.E. / Wucherpfennig, K.W. / Chou, J.J. | ||||||
![]() | ![]() Title: The structural basis for intramembrane assembly of an activating immunoreceptor complex. Authors: Call, M.E. / Wucherpfennig, K.W. / Chou, J.J. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 419.1 KB | Display | ![]() |
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PDB format | ![]() | 364.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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: 6478.848 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: THE FUSION PROTEIN OF DAP12 (RESIDUES 1-33) AND NKG2C (RESIDUES 35-63) Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 3217.884 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 35-66 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: 20 / pH: 6.8 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 600 MHz |
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Processing
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 | |||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 75 / Conformers submitted total number: 15 / Representative conformer: 1 |