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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Detalles Bibliográficos
Autores principales: 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: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2020
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7673765/
https://www.ncbi.nlm.nih.gov/pubmed/33188023
http://dx.doi.org/10.1126/sciadv.abc3099

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7673765/
https://www.ncbi.nlm.nih.gov/pubmed/33188023
http://dx.doi.org/10.1126/sciadv.abc3099

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