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Yorodumi- PDB-2m32: Alpha-1 integrin I-domain in complex with GLOGEN triple helical p... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2m32 | ||||||
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Title | Alpha-1 integrin I-domain in complex with GLOGEN triple helical peptide | ||||||
Components |
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Keywords | CELL ADHESION / alpha-1 integrin / I-domain / GLOGEN | ||||||
Function / homology | Function and homology information cellular extravasation / integrin alpha1-beta1 complex / collagen binding involved in cell-matrix adhesion / Other semaphorin interactions / CHL1 interactions / Laminin interactions / basal part of cell / Platelet Adhesion to exposed collagen / integrin complex / cell adhesion mediated by integrin ...cellular extravasation / integrin alpha1-beta1 complex / collagen binding involved in cell-matrix adhesion / Other semaphorin interactions / CHL1 interactions / Laminin interactions / basal part of cell / Platelet Adhesion to exposed collagen / integrin complex / cell adhesion mediated by integrin / negative regulation of epidermal growth factor receptor signaling pathway / positive regulation of phosphoprotein phosphatase activity / Smooth Muscle Contraction / Integrin cell surface interactions / collagen binding / cell-matrix adhesion / neutrophil chemotaxis / neuron projection morphogenesis / acrosomal vesicle / integrin-mediated signaling pathway / cell-cell adhesion / vasodilation / positive regulation of neuron apoptotic process / integrin binding / perikaryon / protein phosphatase binding / positive regulation of MAPK cascade / negative regulation of cell population proliferation / external side of plasma membrane / focal adhesion / cell surface / extracellular exosome / membrane / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Chin, Y. / Headey, S. / Mohanty, B. / McEwan, P. / Swarbrick, J. / Mulhern, T. / Emsley, J. / Simpson, J. / Scanlon, M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2013 Title: The Structure of Integrin alpha 1I Domain in Complex with a Collagen-mimetic Peptide. Authors: Chin, Y.K. / Headey, S.J. / Mohanty, B. / Patil, R. / McEwan, P.A. / Swarbrick, J.D. / Mulhern, T.D. / Emsley, J. / Simpson, J.S. / Scanlon, M.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2m32.cif.gz | 815.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2m32.ent.gz | 709.9 KB | Display | PDB format |
PDBx/mmJSON format | 2m32.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m3/2m32 ftp://data.pdbj.org/pub/pdb/validation_reports/m3/2m32 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 21513.334 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ITGA1 / Production host: Escherichia coli (E. coli) / References: UniProt: P56199 | ||
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#2: Protein/peptide | Mass: 1962.060 Da / Num. of mol.: 3 / Source method: obtained synthetically / Details: synthetically obtained #3: Chemical | ChemComp-MG / | |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.2 mM [U-98% 13C; U-98% 15N] Alpha-1 integrin, 2.4 mM GLOGEN, 50 mM HEPES, 50 mM NaCl, 5 mM MgCl2, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.1 / pH: 7.4 / Pressure: ambient / Temperature: 298 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: 200 / Conformers submitted total number: 10 |