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. Author manuscript; available in PMC: 2019 Apr 15.
Published in final edited form as: J Phys Chem B. 2018 Aug 8;122(49):11137–11146. doi: 10.1021/acs.jpcb.8b05982

Figure 1.

Figure 1.

Structures and sequences of CaM, nSH2, and cSH2 domains in the p85α subunit. CaM is a symmetric molecule, with two lobes (N- and C-lobe) connected by a flexible linker. The N- and C-lobes each have a hydrophobic pocket, and the linker is populated with residues with negative charges. The nSH2 and cSH2 domains share similar overall structures with a β-sheet bundle surrounded by two α-helixes, but have different amino acid sequences. In the protein sequences, hydrophobic, polar/glycine, positively charged, and negatively charged residues are colored black, green, blue, and red, respectively.