The structure-function relationship of oncogenic LMTK3

Elucidating signaling driven by lemur tyrosine kinase 3 (LMTK3) could help drug development. Here, we solve the crystal structure of LMTK3 kinase domain to 2.1Å resolution, determine its consensus motif and phosphoproteome, unveiling in vitro and in vivo LMTK3 substrates. Via high-throughput homogen...

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Библиографические подробности
Опубликовано в: :Sci Adv
Главные авторы: Ditsiou, Angeliki, Cilibrasi, Chiara, Simigdala, Nikiana, Papakyriakou, Athanasios, Milton-Harris, Leanne, Vella, Viviana, Nettleship, Joanne E., Lo, Jae Ho, Soni, Shivani, Smbatyan, Goar, Ntavelou, Panagiota, Gagliano, Teresa, Iachini, Maria Chiara, Khurshid, Sahir, Simon, Thomas, Zhou, Lihong, Hassell-Hart, Storm, Carter, Philip, Pearl, Laurence H., Owen, Robin L., Owens, Raymond J., Roe, S. Mark, Chayen, Naomi E., Lenz, Heinz-Josef, Spencer, John, Prodromou, Chrisostomos, Klinakis, Apostolos, Stebbing, Justin, Giamas, Georgios
Формат: Artigo
Язык:Inglês
Опубликовано: American Association for the Advancement of Science 2020
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Research Articles
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC7673765/
https://ncbi.nlm.nih.gov/pubmed/33188023
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1126/sciadv.abc3099
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