ArticleThe Journal of biological chemistry2015
The olfactomedin domain from gliomedin is a β-propeller with unique structural properties.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- Blood diagnostic biomarkers for neurologic manifestations of long COVID.Brain, behavior, & immunity - health · 2025Article
- Olfactomedin 4 in cancer development and progression.Biochimica et biophysica acta. Reviews on cancer · 2025Review
- The Ycf48 accessory factor occupies the site of the oxygen-evolving manganese cluster during photosystem II biogenesis.Nature communications · 2023Article
- Mechanisms of node of Ranvier assembly.Nature reviews. Neuroscience · 2021Review
- Olfactomedin-3 Enhances Seizure Activity by Interacting With AMPA Receptors in Epilepsy Models.Frontiers in cell and developmental biology · 2020Article
- Influence of Liver Fibrosis on Lobular Zonation.Cells · 2019Article
- Design and structural characterisation of olfactomedin-1 variants as tools for functional studies.BMC molecular and cell biology · 2019Article
- Calcium-ligand variants of the myocilin olfactomedin propeller selected from invertebrate phyla reveal cross-talk with N-terminal blade and surface helices.Acta crystallographica. Section D, Structural biology · 2019Article
- Stable calcium-free myocilin olfactomedin domain variants reveal challenges in differentiating between benign and glaucoma-causing mutations.The Journal of biological chemistry · 2019Article
- Article
- Survival among children with "Lethal" congenital contracture syndrome 11 caused by novel mutations in the gliomedin gene (GLDN).Human mutation · 2017Article
- Crystallographic anomalous diffraction data for the experimental phasing of two myelin proteins, gliomedin and periaxin.Data in brief · 2017Article
- Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion.Structure (London, England : 1993) · 2015Article
- Structural and Mechanistic Insights into the Latrophilin3-FLRT3 Complex that Mediates Glutamatergic Synapse Development.Structure (London, England : 1993) · 2015Article
- Olfactomedin-1 Has a V-shaped Disulfide-linked Tetrameric Structure.The Journal of biological chemistry · 2015Article
- Molecular Details of Olfactomedin Domains Provide Pathway to Structure-Function Studies.PloS one · 2015Article
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Authors and funding
2 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
All members of the olfactomedin (OLF) family have a conserved extracellular OLF domain, for which a structure has not been available. We present here the crystal structure of the OLF domain from gliomedin. Gliomedin is a protein expressed by Schwann cells in peripheral nerves, important for the formation of the nodes of Ranvier. Gliomedin interacts with neuronal cell adhesion molecules, such as neurofascin, but the structural details of the interaction are not known. The structure of the OLF domain presents a five-bladed β-propeller fold with unusual geometric properties. The symmetry of the structure is not 5-fold, but rather reveals a twisted arrangement. The conserved top face of the gliomedin OLF domain is likely to be important for binding to neuronal ligands. Our results provide a structural basis for the functions of gliomedin in Schwann cells, enable the understanding of the role of the gliomedin OLF domain in autoimmune neuropathies, and unravel the locations of human disease-causing mutations in other OLF family members, including myocilin.
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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.