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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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![]() | SIGNALING PROTEIN / TRANSFERASE / SH2-SH3 interaction | ||||||
Function / homology | ![]() 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 / cell adhesion mediator activity / positive regulation of dendritic cell chemotaxis / negative regulation of hydrogen peroxide biosynthetic process / response to singlet oxygen ...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 / cell adhesion mediator activity / 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 / natural killer cell differentiation / perinuclear endoplasmic reticulum / NTRK2 activates RAC1 / growth factor receptor binding / heart process / regulation of glutamate receptor signaling pathway / Activated NTRK2 signals through FYN / positive regulation of natural killer cell mediated cytotoxicity / reelin-mediated signaling pathway / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / regulation of calcium ion import across plasma membrane / negative regulation of interleukin-12 production / Co-stimulation by CD28 / Platelet Adhesion to exposed collagen / positive regulation of protein localization to membrane / cellular response to L-glutamate / G protein-coupled glutamate receptor signaling pathway / CRMPs in Sema3A signaling / activated T cell proliferation / FLT3 signaling through SRC family kinases / type 5 metabotropic glutamate receptor binding / Nef and signal transduction / negative regulation of dendritic spine maintenance / feeding behavior / Nephrin family interactions / natural killer cell activation / DCC mediated attractive signaling / EPH-Ephrin signaling / Ephrin signaling / dendritic spine maintenance / CD28 dependent Vav1 pathway / dendrite morphogenesis / Regulation of KIT signaling / leukocyte migration / natural killer cell mediated cytotoxicity / phospholipase activator activity / tau-protein kinase activity / Co-inhibition by CTLA4 / negative regulation of T cell receptor signaling pathway / EPHA-mediated growth cone collapse / positive regulation of macrophage chemotaxis / Dectin-2 family / stimulatory C-type lectin receptor signaling pathway / positive regulation of activated T cell proliferation / Fc-gamma receptor signaling pathway involved in phagocytosis / phospholipase binding / response to amyloid-beta / PECAM1 interactions / negative regulation of interleukin-6 production / CD28 dependent PI3K/Akt signaling / negative regulation of type II interferon production / humoral immune response / glial cell projection / FCGR activation / cellular response to glycine / negative regulation of tumor necrosis factor production / ephrin receptor signaling pathway / Sema3A PAK dependent Axon repulsion / positive regulation of protein targeting to membrane / EPH-ephrin mediated repulsion of cells / alpha-tubulin binding / Role of LAT2/NTAL/LAB on calcium mobilization / regulation of immune response / vascular endothelial growth factor receptor signaling pathway / regulation of peptidyl-tyrosine phosphorylation / cellular defense response / detection of mechanical stimulus involved in sensory perception of pain / phagocytosis / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / forebrain development / antigen binding / cellular response to transforming growth factor beta stimulus / GPVI-mediated activation cascade / phagocytic vesicle / cellular response to platelet-derived growth factor stimulus / T cell costimulation / Signaling by ERBB2 / ephrin receptor binding / EPHB-mediated forward signaling / negative regulation of protein ubiquitination / CD209 (DC-SIGN) signaling / NCAM signaling for neurite out-growth / SH2 domain binding / FCGR3A-mediated IL10 synthesis / negative regulation of angiogenesis / axon guidance / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Chan, B. / Griesbach, J. / Song, H.K. / Poy, F. / Terhorst, C. / Eck, M.J. | ||||||
![]() | ![]() Title: 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 49.4 KB | Display | ![]() |
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PDB format | ![]() | 35.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 461.3 KB | Display | ![]() |
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Full document | ![]() | 463.6 KB | Display | |
Data in XML | ![]() | 10.6 KB | Display | |
Data in CIF | ![]() | 13.6 KB | Display | |
Arichive directory | ![]() ![]() | 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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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.) ![]() ![]() ![]() |
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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.) ![]() ![]() ![]() |
#4: Chemical | ChemComp-FLC / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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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: ![]() |
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: ![]()
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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 |