A robust methodology to subclassify pseudokinases based on their nucleotide-binding properties

• Published in: Biochemical journal Vol. 457; no. 2; p. 323
• Main Authors: Murphy, James M, Zhang, Qingwei, Young, Samuel N, Reese, Michael L, Bailey, Fiona P, Eyers, Patrick A, Ungureanu, Daniela, Hammaren, Henrik, Silvennoinen, Olli, Varghese, Leila N, Chen, Kelan, Tripaydonis, Anne, Jura, Natalia, Fukuda, Koichi, Qin, Jun, Nimchuk, Zachary, Mudgett, Mary Beth, Elowe, Sabine, Gee, Christine L, Liu, Ling, Daly, Roger J, Manning, Gerard, Babon, Jeffrey J, Lucet, Isabelle S
• Format: Journal Article
• Language: English
• Published: England 15.01.2014
• Subjects: Amino Acid Sequence; Animals; Cell Line; Humans; Insecta; Janus Kinase 2 - chemistry; Janus Kinase 2 - classification; Janus Kinase 2 - genetics; Molecular Sequence Data; Protein Binding - physiology; Real-Time Polymerase Chain Reaction - methods; Receptor, ErbB-3 - chemistry; Receptor, ErbB-3 - classification; Receptor, ErbB-3 - genetics

Protein kinase-like domains that lack conserved residues known to catalyse phosphoryl transfer, termed pseudokinases, have emerged as important signalling domains across all kingdoms of life. Although predicted to function principally as catalysis-independent protein-interaction modules, several pse...