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Open data
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Basic information
| Entry | Database: PDB / ID: 1m27 | ||||||
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| Title | Crystal structure of SAP/FynSH3/SLAM ternary complex | ||||||
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Keywords | SIGNALING PROTEIN / TRANSFERASE / SH2-SH3 interaction | ||||||
| Function / homology | Function and homology informationnatural killer cell proliferation / negative regulation of CD40 signaling pathway / myeloid dendritic cell activation involved in immune response / negative regulation of T cell cytokine production / regulation of vesicle fusion / leukocyte chemotaxis involved in inflammatory response / positive regulation of dendritic cell chemotaxis / negative regulation of hydrogen peroxide biosynthetic process / response to singlet oxygen / Reelin signalling pathway ...natural killer cell proliferation / negative regulation of CD40 signaling pathway / myeloid dendritic cell activation involved in immune response / negative regulation of T cell cytokine production / regulation of vesicle fusion / leukocyte chemotaxis involved in inflammatory response / positive regulation of dendritic cell chemotaxis / negative regulation of hydrogen peroxide biosynthetic process / response to singlet oxygen / Reelin signalling pathway / positive regulation of T-helper 1 cell cytokine production / perinuclear endoplasmic reticulum / natural killer cell differentiation / NTRK2 activates RAC1 / regulation of glutamate receptor signaling pathway / heart process / Activated NTRK2 signals through FYN / positive regulation of natural killer cell mediated cytotoxicity / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / regulation of calcium ion import across plasma membrane / reelin-mediated signaling pathway / negative regulation of interleukin-12 production / Platelet Adhesion to exposed collagen / CRMPs in Sema3A signaling / G protein-coupled glutamate receptor signaling pathway / FLT3 signaling through SRC family kinases / activated T cell proliferation / positive regulation of protein localization to membrane / type 5 metabotropic glutamate receptor binding / CD4 receptor binding / Nef and signal transduction / feeding behavior / cellular response to L-glutamate / Co-stimulation by CD28 / negative regulation of dendritic spine maintenance / Nephrin family interactions / DCC mediated attractive signaling / natural killer cell activation / EPH-Ephrin signaling / Ephrin signaling / CD28 dependent Vav1 pathway / dendritic spine maintenance / growth factor receptor binding / cellular response to peptide hormone stimulus / tau-protein kinase activity / Regulation of KIT signaling / leukocyte migration / phospholipase activator activity / negative regulation of T cell receptor signaling pathway / Co-inhibition by CTLA4 / natural killer cell mediated cytotoxicity / EPHA-mediated growth cone collapse / peptide hormone receptor binding / dendrite morphogenesis / CD8 receptor binding / Dectin-2 family / positive regulation of macrophage chemotaxis / stimulatory C-type lectin receptor signaling pathway / Fc-gamma receptor signaling pathway involved in phagocytosis / forebrain development / positive regulation of activated T cell proliferation / PECAM1 interactions / response to amyloid-beta / negative regulation of interleukin-6 production / negative regulation of type II interferon production / humoral immune response / cellular response to glycine / FCGR activation / Sema3A PAK dependent Axon repulsion / negative regulation of tumor necrosis factor production / EPH-ephrin mediated repulsion of cells / glial cell projection / CD28 dependent PI3K/Akt signaling / positive regulation of protein targeting to membrane / Role of LAT2/NTAL/LAB on calcium mobilization / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / vascular endothelial growth factor receptor signaling pathway / ephrin receptor signaling pathway / regulation of immune response / detection of mechanical stimulus involved in sensory perception of pain / phagocytosis / alpha-tubulin binding / cellular defense response / cellular response to transforming growth factor beta stimulus / postsynaptic density, intracellular component / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / antigen binding / T cell receptor binding / phospholipase binding / phosphatidylinositol 3-kinase binding / GPVI-mediated activation cascade / ephrin receptor binding / phagocytic vesicle / T cell costimulation / cellular response to platelet-derived growth factor stimulus / Signaling by ERBB2 / negative regulation of protein ubiquitination / EPHB-mediated forward signaling / NCAM signaling for neurite out-growth / CD209 (DC-SIGN) signaling Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Chan, B. / Griesbach, J. / Song, H.K. / Poy, F. / Terhorst, C. / Eck, M.J. | ||||||
Citation | Journal: NAT.CELL BIOL. / Year: 2003Title: SAP couples Fyn to SLAM immune receptors. Authors: Chan, B. / Lanyi, A. / Song, H.K. / Griesbach, J. / Simarro-Grande, M. / Poy, F. / Howie, D. / Sumegi, J. / Terhorst, C. / Eck, M.J. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1m27.cif.gz | 49.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1m27.ent.gz | 35.7 KB | Display | PDB format |
| PDBx/mmJSON format | 1m27.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1m27_validation.pdf.gz | 461.3 KB | Display | wwPDB validaton report |
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| Full document | 1m27_full_validation.pdf.gz | 463.6 KB | Display | |
| Data in XML | 1m27_validation.xml.gz | 10.6 KB | Display | |
| Data in CIF | 1m27_validation.cif.gz | 13.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m2/1m27 ftp://data.pdbj.org/pub/pdb/validation_reports/m2/1m27 | HTTPS FTP |
-Related structure data
| Related structure data | |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
| #1: Protein | Mass: 11702.393 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() |
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| #2: Protein/peptide | Mass: 1280.512 Da / Num. of mol.: 1 / Fragment: SLAM peptide (residues 276-286) / Source method: obtained synthetically Details: This sequence occurs naturally in humans. This sequence was chemically synthesized. References: UniProt: Q13291 |
| #3: Protein | Mass: 6938.519 Da / Num. of mol.: 1 / Fragment: SH3 domain (residues 82-143) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: ![]() |
| #4: Chemical | ChemComp-FLC / |
| #5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.21 Å3/Da / Density % sol: 61.74 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Crystal grow | Temperature: 297 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: Tartrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 297K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Crystal grow | *PLUS Temperature: 22 ℃ / pH: 8 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Diffraction | Mean temperature: 160 K |
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| Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.54 Å |
| Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 20, 2001 / Details: Osmic Mirror |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
| Reflection | Resolution: 2.5→20 Å / Num. all: 62846 / Num. obs: 62846 / % possible obs: 97.8 % / Observed criterion σ(I): -3 |
| Reflection shell | Resolution: 2.5→2.59 Å / % possible all: 98.4 |
| Reflection | *PLUS Lowest resolution: 20 Å / Num. obs: 9233 / % possible obs: 95.5 % / Redundancy: 3.2 % / Num. measured all: 29117 / Rmerge(I) obs: 0.044 |
| Reflection shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.6 Å / % possible obs: 95.5 % / Rmerge(I) obs: 0.246 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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| Refine analyze |
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| Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 2.5→20 Å / Rfactor Rfree error: 0.009
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| Refinement | *PLUS % reflection Rfree: 10 % / Rfactor Rfree: 0.246 / Rfactor Rwork: 0.206 | ||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||
| Displacement parameters | *PLUS | ||||||||||||||||||||
| Refine LS restraints | *PLUS
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| LS refinement shell | *PLUS Lowest resolution: 2.6 Å |
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Homo sapiens (human)
X-RAY DIFFRACTION
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