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. 2018 Mar 7;13(3):e0193947. doi: 10.1371/journal.pone.0193947

Fig 5. Structural model of GCAP1 dimer.

Fig 5

Ribbon diagram of main chain structures of the GCAP1 symmetric dimer (A) and asymmetric dimer (B) that are both consistent with DEER intermolecular distances for spin-label attached to E57C, E133C and E154C. Exposed residues mutated to Cys for DEER studies (E57, E133 and E154) are colored red in panels A and B. Myristoyl group is highlighted magenta. (C) Close-up view of the symmetric dimer showing hydrophobic residues (side-chains of H19, Y22, and V77 colored yellow) at the dimer interface. (D) Close-up view of the symmetric dimer showing intermolecular hydrophobic contacts between Y22, F73, V77 and W94. (E) Close-up view of the asymmetric dimer showing hydrophobic residues (H19, Y22, and V77 colored yellow) at the dimer interface.