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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Detalhes bibliográficos
Publicado no:Sci Adv
Main Authors: 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
Formato: Artigo
Idioma:Inglês
Publicado em: American Association for the Advancement of Science 2020
Assuntos:
Research Articles
Acesso em linha: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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