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Yorodumi- PDB-2v9t: Complex between the second LRR domain of Slit2 and The first Ig d... -
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-Basic information
Entry | Database: PDB / ID: 2v9t | ||||||
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Title | Complex between the second LRR domain of Slit2 and The first Ig domain from Robo1 | ||||||
Components |
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Keywords | STRUCTURAL PROTEIN/RECEPTOR / STRUCTURAL PROTEIN-RECEPTOR COMPLEX / DEVELOPMENTAL PROTEIN / IG DOMAIN / ROUNDABOUT / CHEMOTAXIS / LRR DOMAIN / IMMUNOGLOBULIN DOMAIN / LEUCINE-RICH REPEAT / NEURONAL DEVELOPMENT / PHOSPHORYLATION / EGF-LIKE DOMAIN / DISEASE MUTATION / SLIT2 / LIGAND / MEMBRANE / SECRETED / RECEPTOR / NEUROGENESIS / GLYCOPROTEIN / TRANSMEMBRANE / PROTO-ONCOGENE / DIFFERENTIATION STRUCTURAL PROTEIN/RECEPTOR / COMPLEX | ||||||
Function / homology | Function and homology information negative regulation of leukocyte chemotaxis / corticospinal neuron axon guidance through spinal cord / negative regulation of mononuclear cell migration / negative regulation of lamellipodium assembly / induction of negative chemotaxis / negative regulation of retinal ganglion cell axon guidance / apoptotic process involved in luteolysis / negative regulation of monocyte chemotaxis / chemorepulsion involved in postnatal olfactory bulb interneuron migration / Roundabout binding ...negative regulation of leukocyte chemotaxis / corticospinal neuron axon guidance through spinal cord / negative regulation of mononuclear cell migration / negative regulation of lamellipodium assembly / induction of negative chemotaxis / negative regulation of retinal ganglion cell axon guidance / apoptotic process involved in luteolysis / negative regulation of monocyte chemotaxis / chemorepulsion involved in postnatal olfactory bulb interneuron migration / Roundabout binding / negative regulation of negative chemotaxis / negative regulation of smooth muscle cell chemotaxis / negative regulation of cellular response to growth factor stimulus / Regulation of cortical dendrite branching / cellular response to heparin / negative regulation of small GTPase mediated signal transduction / negative regulation of mammary gland epithelial cell proliferation / LRR domain binding / negative regulation of chemokine-mediated signaling pathway / response to cortisol / laminin-1 binding / negative regulation of smooth muscle cell migration / heart induction / axon extension involved in axon guidance / axon guidance receptor activity / positive regulation of vascular endothelial growth factor signaling pathway / Netrin-1 signaling / GTPase inhibitor activity / Regulation of commissural axon pathfinding by SLIT and ROBO / Role of ABL in ROBO-SLIT signaling / Inactivation of CDC42 and RAC1 / negative regulation of neutrophil chemotaxis / SLIT2:ROBO1 increases RHOA activity / Roundabout signaling pathway / endocardial cushion formation / negative regulation of actin filament polymerization / Signaling by ROBO receptors / pulmonary valve morphogenesis / outflow tract septum morphogenesis / negative regulation of vascular permeability / motor neuron axon guidance / cell migration involved in sprouting angiogenesis / aortic valve morphogenesis / retinal ganglion cell axon guidance / Activation of RAC1 / positive regulation of vascular endothelial growth factor receptor signaling pathway / axon midline choice point recognition / aorta development / ureteric bud development / proteoglycan binding / negative regulation of endothelial cell migration / positive regulation of Rho protein signal transduction / negative chemotaxis / positive regulation of axonogenesis / ventricular septum morphogenesis / branching morphogenesis of an epithelial tube / positive regulation of Notch signaling pathway / homophilic cell adhesion via plasma membrane adhesion molecules / cellular response to hormone stimulus / endoplasmic reticulum-Golgi intermediate compartment membrane / negative regulation of cell migration / negative regulation of protein phosphorylation / axon guidance / positive regulation of MAP kinase activity / negative regulation of cell growth / Regulation of expression of SLITs and ROBOs / activation of cysteine-type endopeptidase activity involved in apoptotic process / heparin binding / nervous system development / cell adhesion / neuron projection / positive regulation of apoptotic process / axon / negative regulation of gene expression / calcium ion binding / positive regulation of gene expression / cell surface / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / membrane / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Morlot, C. / Cusack, S. / McCarthy, A.A. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2007 Title: Structural Insights Into the Slit-Robo Complex. Authors: Morlot, C. / Thielens, N.M. / Ravelli, R.B. / Hemrika, W. / Romijn, R.A. / Gros, P. / Cusack, S. / Mccarthy, A.A. #1: Journal: Acta Crystallogr.,Sect.F / Year: 2007 Title: Cloning, Expression, Crystallization and Preliminary X-Ray Analysis of the First Two Ig Domains from Human Roundabout 1 (Robo1). Authors: Morlot, C. / Hemrika, W. / Romijn, R.A. / Gros, P. / Cusack, S. / Mccarthy, A.A. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2v9t.cif.gz | 81.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2v9t.ent.gz | 64.2 KB | Display | PDB format |
PDBx/mmJSON format | 2v9t.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v9/2v9t ftp://data.pdbj.org/pub/pdb/validation_reports/v9/2v9t | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 13103.687 Da / Num. of mol.: 1 / Fragment: IG1-2M, RESIDUES 61-166 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): HEK293-EBNA1 / Production host: HOMO SAPIENS (human) / References: UniProt: Q9Y6N7 | ||
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#2: Protein | Mass: 24676.551 Da / Num. of mol.: 1 / Fragment: SECOND LRR DOMAIN, RESIDUES 271-479 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Cell line (production host): HEK293-EBNA1 / Production host: HOMO SAPIENS (human) / References: UniProt: O94813 | ||
#3: Water | ChemComp-HOH / | ||
Compound details | ENGINEEREDSequence details | A N160D MUTATION WAS MADE TO PREVENT POTENTIAL GLYCOSYLAT | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 53 % / Description: NONE |
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Crystal grow | pH: 5.6 / Details: 12% PEG 6000, 0.1M LI SO4, 0.1M NA CITRATE, PH=5.6 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9537 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jan 26, 2007 / Details: TORODIAL MIRROR |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→30 Å / Num. obs: 42371 / % possible obs: 98.1 % / Observed criterion σ(I): 1 / Redundancy: 3.8 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 12.9 |
Reflection shell | Resolution: 1.7→1.8 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.53 / Mean I/σ(I) obs: 2.5 / % possible all: 94.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.7→19.98 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.938 / SU B: 4.559 / SU ML: 0.077 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.1 / ESU R Free: 0.103 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.96 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→19.98 Å
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