ArticleThe Journal of biological chemistry2015
Olfactomedin-1 Has a V-shaped Disulfide-linked Tetrameric Structure.
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 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Gating and noelin clustering of native CaNature · 2025Article
- Article
- LRFN5 and OLFM4 as novel potential biomarkers for major depressive disorder: a pilot study.Translational psychiatry · 2023Article
- Molecular architecture and modifications of full-length myocilin.Experimental eye research · 2021Article
- Article
- Olfactomedin-3 Enhances Seizure Activity by Interacting With AMPA Receptors in Epilepsy Models.Frontiers in cell and developmental biology · 2020Article
- 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
- Noelin1 Affects Lateral Mobility of Synaptic AMPA Receptors.Cell reports · 2018Article
- Structure and Misfolding of the Flexible Tripartite Coiled-Coil Domain of Glaucoma-Associated Myocilin.Structure (London, England : 1993) · 2017Article
- Mutated olfactomedin 1 in the interphotoreceptor matrix of the mouse retina causes functional deficits and vulnerability to light damage.Histochemistry and cell biology · 2017Article
- Structural and Mechanistic Insights into the Latrophilin3-FLRT3 Complex that Mediates Glutamatergic Synapse Development.Structure (London, England : 1993) · 2015Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Olfactomedin-1 (Olfm1; also known as noelin and pancortin) is a member of the olfactomedin domain-containing superfamily and a highly expressed neuronal glycoprotein important for nervous system development. It binds a number of secreted proteins and cell surface-bound receptors to induce cell signaling processes. Using a combined approach of x-ray crystallography, solution scattering, analytical ultracentrifugation, and electron microscopy we determined that full-length Olfm1 forms disulfide-linked tetramers with a distinctive V-shaped architecture. The base of the "V" is formed by two disulfide-linked dimeric N-terminal domains. Each of the two V legs consists of a parallel dimeric disulfide-linked coiled coil with a C-terminal β-propeller dimer at the tips. This agrees with our crystal structure of a C-terminal coiled-coil segment and β-propeller combination (Olfm1(coil-Olf)) that reveals a disulfide-linked dimeric arrangement with the β-propeller top faces in an outward exposed orientation. Similar to its family member myocilin, Olfm1 is stabilized by calcium. The dimer-of-dimers architecture suggests a role for Olfm1 in clustering receptors to regulate signaling and sheds light on the conformation of several other olfactomedin domain family members.
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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.