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. 2005 May 13;89(2):1214–1226. doi: 10.1529/biophysj.104.055780

FIGURE 1.

FIGURE 1

A schematic model of the CaM:SEF2-1mp complex based on intermolecular CaM:CaM contacts and the 2:2 stoichiometry (11). The CaM molecules (orange) create a dimer where the C-terminal domain of one CaM contacts the N-terminal of the other CaM, which creates a hydrophobic tunnel. Inside the tunnel the dimeric SEF2-1mp peptide (blue) is trapped, and is in constant exchange between different bound conformations. In addition, the CaM domains undergo a wobbling motion with a correlation time of ∼2.5 ns. This figure should, therefore, not be interpreted as a fixed localization of SEF2-1mp.