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Yorodumi- PDB-2lmf: Solution structure of human LL-23 bound to membrane-mimetic micelles -
+Open data
-Basic information
Entry | Database: PDB / ID: 2lmf | ||||||
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Title | Solution structure of human LL-23 bound to membrane-mimetic micelles | ||||||
Components | Antibacterial protein LL-37Antibiotic | ||||||
Keywords | ANTIMICROBIAL PROTEIN / antimicrobial and innate immune modulating peptide | ||||||
Function / homology | Function and homology information cytolysis / killing by host of symbiont cells / neutrophil activation / specific granule / cellular response to peptidoglycan / cellular response to interleukin-6 / Antimicrobial peptides / cellular response to interleukin-1 / innate immune response in mucosa / cell projection ...cytolysis / killing by host of symbiont cells / neutrophil activation / specific granule / cellular response to peptidoglycan / cellular response to interleukin-6 / Antimicrobial peptides / cellular response to interleukin-1 / innate immune response in mucosa / cell projection / lipopolysaccharide binding / specific granule lumen / positive regulation of angiogenesis / antimicrobial humoral immune response mediated by antimicrobial peptide / tertiary granule lumen / cellular response to tumor necrosis factor / antibacterial humoral response / cellular response to lipopolysaccharide / defense response to Gram-negative bacterium / amyloid fibril formation / defense response to Gram-positive bacterium / defense response to bacterium / positive regulation of protein phosphorylation / innate immune response / positive regulation of cell population proliferation / Neutrophil degranulation / extracellular space / extracellular exosome / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 20 | ||||||
Authors | Wang, G. | ||||||
Citation | Journal: Biochemistry / Year: 2012 Title: Structure, Dynamics, and Antimicrobial and Immune Modulatory Activities of Human LL-23 and Its Single-Residue Variants Mutated on the Basis of Homologous Primate Cathelicidins. Authors: Wang, G. / Elliott, M. / Cogen, A.L. / Ezell, E.L. / Gallo, R.L. / Hancock, R.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lmf.cif.gz | 163.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lmf.ent.gz | 136.4 KB | Display | PDB format |
PDBx/mmJSON format | 2lmf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lm/2lmf ftp://data.pdbj.org/pub/pdb/validation_reports/lm/2lmf | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2831.405 Da / Num. of mol.: 1 / Fragment: UNP residues 134-156 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P49913 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 2 mM LL, 100% D2O / Solvent system: 100% D2O |
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Sample | Conc.: 2 mM / Component: LL-23-1 |
Sample conditions | Ionic strength: unbuffered / pH: 6 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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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 |