ArticleStructure (London, England : 1993)2020
Drosophila OTK Is a Glycosaminoglycan-Binding Protein with High Conformational Flexibility.
Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Expanding ligand-receptor interaction networks for axon guidance: Structural insights into signal crosstalk and specificity.Current opinion in neurobiology · 2025Review
- Molecular mechanisms of proteoglycan-mediated semaphorin signaling in axon guidance.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- RHAMM Is a Multifunctional Protein That Regulates Cancer Progression.International journal of molecular sciences · 2021Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The transmembrane protein OTK plays an essential role in plexin and Wnt signaling during Drosophila development. We have determined a crystal structure of the last three domains of the OTK ectodomain and found that OTK shows high conformational flexibility resulting from mobility at the interdomain interfaces. We failed to detect direct binding between Drosophila Plexin A (PlexA) and OTK, which was suggested previously. We found that, instead of PlexA, OTK directly binds semaphorin 1a. Our binding analyses further revealed that glycosaminoglycans, heparin and heparan sulfate, are ligands for OTK and thus may play a role in the Sema1a-PlexA axon guidance system.
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