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Interaction of recombinant soluble neuroligins-1 with neurexin-beta


Interaction of recombinant soluble neuroligins-1 with neurexin-beta



FASEB Journal 17(4-5): Abstract 395



ISSN/ISBN: 0892-6638

Neuroligins are postsynaptic transmembrane proteins of the alpha/beta-hydrolase fold family that form heterologous cell contacts with the neurexin-beta family. To examine neuroligin-1 (NL1) interactions with neurexin1-beta (NX1beta), we expressed soluble, recombinant forms of NL1 by truncating the carboxyl-terminal end prior to the transmembrane span at positions D638 and D691. NL1 truncated at D691 was crystallized by vapor diffusion and data up to 4.35 A were collected on the ESRF beamline ID29. Attempts to solve the structure by molecular replacement were unsuccessful but efforts to solve a structure of a truncated NL1 devoid of O-glycans are underway. By sedimentation equilibrium we determined that both NL1 forms behave as dimer in solution with a calculated Mr of about 173 (D691)and 165 (D638) kDa. By surface plasmon resonance, we studied the association of purified NLs with NX1beta. Both truncated mutants associate with NX1beta with a nM KD, while the homologous protein AChE does not bind NX1beta. Moreover, NL1 binds the two splice site 4 forms of NX1beta with slight differences in affinity. Incomplete post-translational processing of NL1 and enzymatic removal of certain oligosaccharides or sialic acids enhance activity, while enzymatic deglycosylation of NX1beta does not alter binding, indicating that glycosylation of NL1 may provide a further level of control in the neurexin-neuroligin association. (GM-18360 to P.T.).

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Accession: 035156423

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