ArticleStructure (London, England : 1993)2011
The crystal structure of the α-neurexin-1 extracellular region reveals a hinge point for mediating synaptic adhesion and function.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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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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45 citing papers in PubMed, 68 citations in OpenAlex.
- Review
- Biallelic variants in CELSR1 cause brain malformations, neurodevelopmental disorders and epilepsy in humans.Nature communications · 2026Article
- Patient-Derived Variants Define Constraints for Ligand Binding at the PDZ Domain of CASK.Journal of neurochemistry · 2025Article
- Unveiling proteomic and peptide-level modifications in cerebrospinal fluid and plasma in normal cognitive aging.Communications medicine · 2025Article
- Alpha-neurexins in health and disease.Frontiers in molecular neuroscience · 2025Review
- A Systematic Structure-Function Characterization of a Human Mutation in Neurexin-3α Reveals an Extracellular Modulatory Sequence That Stabilizes Neuroligin-1 Binding to Enhance the Postsynaptic Properties of Excitatory Synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024Article
- Structural basis of α-latrotoxin transition to a cation-selective pore.Nature communications · 2024Article
- Neuronal and non-neuronal functions of the synaptic cell adhesion molecule neurexin in Nematostella vectensis.Nature communications · 2024Article
- Landscape ofJournal of clinical medicine · 2024Review
- Article
- Neurexins: molecular codes for shaping neuronal synapses.Nature reviews. Neuroscience · 2021Review
- The Ig-like domain of Punctin/MADD-4 is the primary determinant for interaction with the ectodomain of neuroligin NLG-1.The Journal of biological chemistry · 2020Article
- Functional characterization of rare NRXN1 variants identified in autism spectrum disorders and schizophrenia.Journal of neurodevelopmental disorders · 2020Article
- Structures of neurexophilin-neurexin complexes reveal a regulatory mechanism of alternative splicing.The EMBO journal · 2019Article
- Modeling a Neurexin-3α Human Mutation in Mouse Neurons Identifies a Novel Role in the Regulation of Transsynaptic Signaling and Neurotransmitter Release at Excitatory Synapses.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- Genetic insights and neurobiological implications from NRXN1 in neuropsychiatric disorders.Molecular psychiatry · 2019Review
- Candidate CSPG4 mutations and induced pluripotent stem cell modeling implicate oligodendrocyte progenitor cell dysfunction in familial schizophrenia.Molecular psychiatry · 2019Article
- Neurexins - versatile molecular platforms in the synaptic cleft.Current opinion in structural biology · 2019Review
- Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer.Journal of molecular biology · 2018Article
- Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains-A Structural Perspective.Molecules (Basel, Switzerland) · 2017Review
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6 authors at 1 institution in 2 countries.
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Abstract
α- and β-neurexins (NRXNs) are transmembrane cell adhesion proteins that localize to presynaptic membranes in neurons and interact with the postsynaptic neuroligins (NLGNs). Their gene mutations are associated with the autism spectrum disorders. The extracellular region of α-NRXNs, containing nine independently folded domains, has structural complexity and unique functional characteristics, distinguishing it from the smaller β-NRXNs. We have solved the X-ray crystal structure of seven contiguous domains of the α-NRXN-1 extracellular region at 3.0 Å resolution. The structure reveals an arrangement where the N-terminal five domains adopt a more rigid linear conformation and the two C-terminal domains form a separate arm connected by a flexible hinge. In an extended conformation the molecule is suitably configured to accommodate a bound NLGN molecule, as supported by structural comparison and surface plasmon resonance. These studies provide the structural basis for a multifunctional synaptic adhesion complex mediated by α-NRXN-1.
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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.