期刊
STRUCTURE
卷 28, 期 5, 页码 507-+出版社
CELL PRESS
DOI: 10.1016/j.str.2020.02.008
关键词
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资金
- Cancer Research UK, United Kingdom
- Medical Research Council Programme Grants, United Kingdom [C375/A17721, MR/M000141/1]
- Wellcome Trust Centre grant, United Kingdom [203141/Z/16/Z]
- EMBO Long-Term Fellowship, Germany [ALTF 604-2014, ALTF 1061-2017]
- Nuffield Department of Medicine Leadership Fellowship, United Kingdom
- MRC [MR/M000141/1] Funding Source: UKRI
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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