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TitleCrystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding.
Journal, issue, pagesBiochemistry, Vol. 55, Issue 6, Page 914-926, Year 2016
Publish dateFeb 16, 2016
AuthorsAnja Paatero / Katja Rosti / Alexander V Shkumatov / Celeste Sele / Cecilia Brunello / Kai Kysenius / Prosanta Singha / Ville Jokinen / Henri Huttunen / Tommi Kajander /
PubMed AbstractSynaptic 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.
External linksBiochemistry / PubMed:26785044
MethodsSAS (X-ray synchrotron) / X-ray diffraction
Resolution2.097 Å
Structure data

SASDBG3:
Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)
Method: SAXS/SANS

SASDBH3:
Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 (fragment 30-380)
Method: SAXS/SANS

PDB-5a5c:
Structure of an engineered neuronal LRRTM2 adhesion molecule
Method: X-RAY DIFFRACTION / Resolution: 2.097 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • Mus musculus (house mouse)
  • synthetic construct (others)
KeywordsSIGNALING PROTEIN / LRRTM / SYNAPSE / ADHESION / LEUCINE RICH REPEAT / NEUREXIN

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