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. Author manuscript; available in PMC: 2015 Jan 23.
Published in final edited form as: J Mol Biol. 2013 Oct 6;426(2):423–435. doi: 10.1016/j.jmb.2013.10.001

Figure 1.

Figure 1

Figure 1

(A) Auto-inhibited conformation of c-Src kinase. From N-terminus to C-terminus, this figure shows SH3 domain (in yellow), a connector between SH2 and SH3 domains (in cyan), SH2 domain (in green), linker region which connects SH2 and kinase domains (in purple), the kinase domain (in blue), and the C-terminal tail which contains Y527 (in red). In the auto-inhibited conformation, SH3 domain binds linker, SH2 domain binds phosphorylated Y527. (B) Reassembled active-like conformation of c-Src kinase. The same color code used previously is adopted here. In the reassembled active-like conformation, SH3 domain unbinds the linker, SH2 domain unbinds Y527, and Y527 is not phosphorylated. (C) Sequence of the construct that is used in the simulations. Important residues and motifs that will be analyzed are colored.