ArticleProceedings of the National Academy of Sciences of the United States of America2008
Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- Neuroligins and Neuropathic Pain: Insights into Synaptic Plasticity and Pain Transmission.Biology · 2026Review
- Weaker neuroligin 2-neurexin β1 interaction tethers membranes and recruits gephyrin at membrane junctions through clustering.Science advances · 2026Article
- Region-Specific Phosphorylation Determines Neuroligin-3 Localization to Excitatory Versus Inhibitory Synapses.Biological psychiatry · 2024Article
- Expression and structural analysis of human neuroligin 2 and neuroligin 3 implicated in autism spectrum disorders.Frontiers in endocrinology · 2022Article
- Canonical versus non-canonical transsynaptic signaling of neuroligin 3 tunes development of sociality in mice.Nature communications · 2021Article
- Neurexins: molecular codes for shaping neuronal synapses.Nature reviews. Neuroscience · 2021Review
- An Autism-Associated Mutation Impairs Neuroligin-4 Glycosylation and Enhances Excitatory Synaptic Transmission in Human Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- NL1 expression level in Nrx1β and the excitability of PV interneurons in mice with POCD.Experimental and therapeutic medicine · 2019Article
- Posttranslational modifications of neuroligins regulate neuronal and glial signaling.Current opinion in neurobiology · 2017Review
- Molecular Mechanism of MDGA1: Regulation of Neuroligin 2:Neurexin Trans-synaptic Bridges.Neuron · 2017Article
- The cellular and molecular landscape of neuroligins.Trends in neurosciences · 2015Review
- Physical Interactions and Functional Relationships of Neuroligin 2 and Midbrain Serotonin Transporters.Frontiers in synaptic neuroscience · 2015Article
- Dystroglycan binding to α-neurexin competes with neurexophilin-1 and neuroligin in the brain.The Journal of biological chemistry · 2014Article
- Conserved and divergent processing of neuroligin and neurexin genes: from the nematode C. elegans to human.Invertebrate neuroscience : IN · 2014Article
- The neuroligins and their ligands: from structure to function at the synapse.Journal of molecular neuroscience : MN · 2014Article
- Variations analysis of NLGN3 and NLGN4X gene in Chinese autism patients.Molecular biology reports · 2014Article
- Impaired hippocampal neuroligin-2 function by chronic stress or synthetic peptide treatment is linked to social deficits and increased aggression.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2014Article
- Neurexins.Genome biology · 2013Review
- Neurexins, neuroligins and LRRTMs: synaptic adhesion getting fishy.Journal of neurochemistry · 2011Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Neuroligins (NLs) are catalytically inactive members of a family of cholinesterase-like transmembrane proteins that mediate cell adhesion at neuronal synapses. Postsynaptic neuroligins engage in Ca2+-dependent transsynaptic interactions via their extracellular cholinesterase domain with presynaptic neurexins (NRXs). These interactions may be regulated by two short splice insertions (termed A and B) in the NL cholinesterase domain. Here, we present the 3.3-A crystal structure of the ectodomain from NL2 containing splice insertion A (NL2A). The overall structure of NL2A resembles that of cholinesterases, but several structural features are unique to the NL proteins. First, structural elements surrounding the esterase active-site region differ significantly between active esterases and NL2A. On the opposite surface of the NL2A molecule, the positions of the A and B splice insertions identify a candidate NRX interaction site of the NL protein. Finally, sequence comparisons of NL isoforms allow for mapping the location of residues of previously identified mutations in NL3 and NL4 found in patients with autism spectrum disorders. Overall, the NL2 structure promises to provide a valuable model for dissecting NL isoform- and synapse-specific functions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.