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Yorodumi- SASDBG3: Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (st... -
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-Basic information
Entry | Database: SASBDB / ID: SASDBG3 |
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Sample | Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)
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Function / homology | Function and homology information : / Neurexins and neuroligins / : / regulation of postsynaptic density assembly / neurexin family protein binding / negative regulation of receptor internalization / anchoring junction / positive regulation of synapse assembly / excitatory synapse / GABA-ergic synapse ...: / Neurexins and neuroligins / : / regulation of postsynaptic density assembly / neurexin family protein binding / negative regulation of receptor internalization / anchoring junction / positive regulation of synapse assembly / excitatory synapse / GABA-ergic synapse / hippocampal mossy fiber to CA3 synapse / long-term synaptic potentiation / synapse organization / Schaffer collateral - CA1 synapse / membrane => GO:0016020 / glutamatergic synapse / extracellular space Similarity search - Function |
Biological species | Mus musculus (house mouse) |
Citation | Journal: Biochemistry / Year: 2016 Title: Crystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding. Authors: Anja Paatero / Katja Rosti / Alexander V Shkumatov / Celeste Sele / Cecilia Brunello / Kai Kysenius / Prosanta Singha / Ville Jokinen / Henri Huttunen / Tommi Kajander / Abstract: Synaptic adhesion molecules are key components in development of the brain, and in the formation of neuronal circuits, as they are central in the assembly and maturation of chemical synapses. Several ...Synaptic adhesion molecules are key components in development of the brain, and in the formation of neuronal circuits, as they are central in the assembly and maturation of chemical synapses. Several families of neuronal adhesion molecules have been identified such as the neuronal cell adhesion molecules, neurexins and neuroligins, and in particular recently several leucine-rich repeat proteins, e.g., Netrin G-ligands, SLITRKs, and LRRTMs. The LRRTMs form a family of four proteins. They have been implicated in excitatory glutamatergic synapse function and were specifically characterized as ligands for neurexins in excitatory synapse formation and maintenance. In addition, LRRTM3 and LRRTM4 have been found to be ligands for heparan sulfate proteoglycans, including glypican. We report here the crystal structure of a thermostabilized mouse LRRTM2, with a Tm 30 °C higher than that of the wild-type protein. We localized the neurexin binding site to the concave surface based on protein engineering, sequence conservation, and prior information about the interaction of the ligand with neurexins, which allowed us to propose a tentative model for the LRRTM-neurexin interaction complex. We also determined affinities of the thermostabilized LRRTM2 and wild-type LRRTM1 and LRRTM2 for neurexin-β1 with and without Ca(2+). Cell culture studies and binding experiments show that the engineered protein is functional and capable of forming synapselike contacts. The structural and functional data presented here provide the first structure of an LRRTM protein and allow us to propose a model for the molecular mechanism of LRRTM function in the synaptic adhesion. |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDBG3 |
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-Related structure data
-External links
Related items in Molecule of the Month |
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-Models
Model #445 | Type: dummy / Radius of dummy atoms: 2.75 A / Chi-square value: 0.700 Search similar-shape structures of this assembly by Omokage search (details) |
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-Sample
Sample | Name: Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct) Specimen concentration: 1.10-5.50 |
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Buffer | Name: 20 mM Tris 150 mM NaCl 3% glycerol / Concentration: 20.00 mM / pH: 7.4 / Composition: 150 mM NaCl, 3% glycerol |
Entity #296 | Name: cLRRTM2 30-380 / Type: protein Description: Mouse Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct) Formula weight: 40.01 / Num. of mol.: 1 / Source: Mus musculus / References: UniProt: Q8BGA3 Sequence: GPMACPPKCR CEKLLFYCDS QGFHSVPNGL PSQLLGLSLR HNQLQSLPNG VFDKLTQLTW LHLDHNQLQS LPNGVFDKLT KLTELILSSN QLQSLPNGTF DKLTNLQNLD LSFNQLQSLP NGVFDKLTNL QTLHLRSNQL QSLPNGVFDK LTSLTFLDLS TNQLQSLPNG ...Sequence: GPMACPPKCR CEKLLFYCDS QGFHSVPNGL PSQLLGLSLR HNQLQSLPNG VFDKLTQLTW LHLDHNQLQS LPNGVFDKLT KLTELILSSN QLQSLPNGTF DKLTNLQNLD LSFNQLQSLP NGVFDKLTNL QTLHLRSNQL QSLPNGVFDK LTSLTFLDLS TNQLQSLPNG VFDKLTNLRE LHLEHNQLQS LPNGVFDKLT SLTTLFLQWN QLQSLPNGVF DKLTNLEKLD LTGNQLQSLP NGVFDKLTNL KILLLDNNQL QSLPNGVFDK LKSLTTVGLS GNLWECSPRV CALASWLGSF QGRWEHSILC HSPDHTQGED ILDAVHGFQL CWNLSTTVTA MATTYRDPTT EKLVEKY |
-Experimental information
Beam | Instrument name: ESRF ID14-3 / City: Grenoble / 国: France / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.09 Å / Dist. spec. to detc.: 2.87 mm | |||||||||||||||
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Detector | Name: Pilatus 1M | |||||||||||||||
Scan | Title: Mouse Leucine-rich TM protein cLRRTM2 (engineered) / Measurement date: Sep 27, 2015 / Storage temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/nm /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 941 /
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Result | D max: 13.1 / Type of curve: single_conc /
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