Abstract
AbstractThe effector BCL‐2 (B cell lymphoma‐2) protein BAK (B cell lymphoma‐2 homologous antagonist/killer) directly mediates mitochondrial outer membrane permeabilization to drive the mitochondrial pathway of apoptosis. The structures of BAK are presented to reveal two different modes of homodimerization. Noncovalent dimerization is mediated by one Zn2+atom to inhibit the release of cytochromecfrom mitochondrial intermembrane space. Covalent oxidative homodimerization occurs through disulfide bond formation at Cys166 and is thought to prevent the Zn2+‐mediated inhibition by abolishing the Zn2+‐dependent homodimerization interface. Neither mode of dimerization affects the putative B cell lymphoma‐2 homology 3 (BH3)‐binding pocket, which remains occluded in BAK to preclude high affinity BH3 peptide binding.
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