Article
Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.
Journal of biochemistry - 1 Nov 2012
Takeshita Kohei, Tezuka Tohru, Isozaki Yukari, Yamashita Eiki, Suzuki Mamoru, Kim Minsoo, Yamanashi Yuji, Yamamoto Tadashi, Nakagawa Atsushi
Abstract excerpt
Through their ubiquitin ligase activity, Cbl-family proteins suppress signalling mediated by protein-tyrosine kinases (PTKs), but can also function as adaptor proteins to positively regulate signalling. The tyrosine kinase binding (TKB) domain of this family is critical for binding with tyrosine-phosphorylated target proteins. Here, we analysed the crystal structure of the TKB domain of Cbl-c/Cbl-3 (Cbl-c TKB),...
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