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Yorodumi- PDB-2jx9: Solution structure of the Gal_lectin domain of mouse Latrophilin-... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2jx9 | ||||||
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Title | Solution structure of the Gal_lectin domain of mouse Latrophilin-1 GPCR | ||||||
Components | Latrophilin 1 | ||||||
Keywords | CELL ADHESION / SIGNALING PROTEIN / Lectin / beta-sandwich / disulphide / glycosylated / G-protein coupled receptor / Membrane / Receptor / Transducer / Transmembrane | ||||||
Function / homology | Function and homology information latrotoxin receptor activity / positive regulation of synapse maturation / positive regulation of synapse assembly / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / toxic substance binding / cell adhesion molecule binding / G protein-coupled receptor activity / adenylate cyclase-activating G protein-coupled receptor signaling pathway / presynaptic membrane / growth cone ...latrotoxin receptor activity / positive regulation of synapse maturation / positive regulation of synapse assembly / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / toxic substance binding / cell adhesion molecule binding / G protein-coupled receptor activity / adenylate cyclase-activating G protein-coupled receptor signaling pathway / presynaptic membrane / growth cone / carbohydrate binding / cell surface receptor signaling pathway / neuron projection / axon / glutamatergic synapse / synapse / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Authors | Vakonakis, I. / Campbell, I.D. | ||||||
Citation | Journal: To be Published Title: Solution structure and sugar-binding mechanism of mouse Latrophilin-1 RBL: a novel 7TM receptor-attached lectin-like domain. Authors: Vakonakis, I. / Langenhan, T. / Promel, S. / Russ, A. / Campbell, I.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jx9.cif.gz | 804.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jx9.ent.gz | 674.6 KB | Display | PDB format |
PDBx/mmJSON format | 2jx9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2jx9_validation.pdf.gz | 573.1 KB | Display | wwPDB validaton report |
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Full document | 2jx9_full_validation.pdf.gz | 882.1 KB | Display | |
Data in XML | 2jx9_validation.xml.gz | 73 KB | Display | |
Data in CIF | 2jx9_validation.cif.gz | 104.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jx/2jx9 ftp://data.pdbj.org/pub/pdb/validation_reports/jx/2jx9 | HTTPS FTP |
-Related structure data
Related structure data | 2jxaC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11997.645 Da / Num. of mol.: 1 / Fragment: Gal_lectin Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) Description: gene construct integrated in the organism's genome Gene: Lphn1 / Production host: Pichia pastoris (fungus) / Strain (production host): X-33 / References: UniProt: Q5U4D5, UniProt: Q80TR1*PLUS |
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#2: Sugar | ChemComp-NAG / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 30 / pH: 7 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 Details: Used to create the structure ensemble, Used for final ensemble refinement | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: Structures with lowest energy / Conformers calculated total number: 50 / Conformers submitted total number: 25 |