6S9F
Drosophila OTK, extracellular domains 3-5
Summary for 6S9F
Entry DOI | 10.2210/pdb6s9f/pdb |
Descriptor | Tyrosine-protein kinase-like otk, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total) |
Functional Keywords | otk, off-track, ig-like domain, signalling, signaling protein |
Biological source | Drosophila melanogaster (Fruit fly) |
Total number of polymer chains | 2 |
Total formula weight | 129606.23 |
Authors | Rozbesky, D.,Jones, E.Y. (deposition date: 2019-07-12, release date: 2020-03-25, Last modification date: 2024-11-20) |
Primary citation | Rozbesky, D.,Monistrol, J.,Jain, V.,Hillier, J.,Padilla-Parra, S.,Jones, E.Y. Drosophila OTK Is a Glycosaminoglycan-Binding Protein with High Conformational Flexibility. Structure, 28:507-515.e5, 2020 Cited by PubMed 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. PubMed: 32187531DOI: 10.1016/j.str.2020.02.008 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.969 Å) |
Structure validation
Download full validation report
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