Biochemistry

Into the Membrane

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Science  01 Feb 2002:
Vol. 295, Issue 5556, pp. 767
DOI: 10.1126/science.295.5556.767b

C2 domains are membrane-docking modules found in many signal transduction and vesicle-trafficking proteins. In many cases, calcium binding regulates membrane association.

Murray and Honig used finite-difference Poisson-Boltzmann calculations to describe the electrostatic interactions of C2 domains of known structure with phospholipid membranes. Nonspecific electrostatic interactions were important for association with both negatively charged and neutral membranes. Calcium provided positive charge that attracted negatively charged membranes and reduced the desolvation penalty associated with membrane binding. Desolvation effects were particularly important in penetration of neutral membranes that in turn facilitate hydrophobic interactions. Calcium-independent C2 domains had similar electrostatic profiles. Quantitative estimates of the effect of experimental variables such as lipid composition, ionic strength, and mutations support a general role for these nonspecific electrostatic interactions. — VV

Mol. Cell9, 145 (2002).

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