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[Cover image of issue]

Cover photograph: Atomistic representation of wild-type (left) and Cys-double-mutant (right) prolactin receptor dimers, showing the quaternary structure arrangements of the extracellular domains (middle; lipid bilayer shown schematically). Spheres indicate cysteines (yellow) and serines (red). The upper panels show relative rearrangements of the C-terminus subdomains upon disulfide bond disruption (views from the extracellular side). The resulting structural changes propagate downward to the N-terminus subdomains (lower panels), impacting JAK2 binding to the intracellular tail of the receptor (view from the membrane side; monomers are blue and green, and Cα atoms of the N terminus are red). The prolactin binding pocket is accessible in the wild type and occluded in the mutant. These changes may explain at the atomic level the nature of the changes derived from biochemical analyses, including homo- and heterodimer association and the inhibitory action of the prolactin receptor short form. (See related article in May 2009, vol. 29, no. 10, p. 2546.)

Mol Cell Biol. 2009 December; 29(24): Cover