Carriers of clusterin risk alleles have an increased likelihood of developing late-onset Alzheimer’s disease (LOAD). In order to better understand the function of the associated protein, researchers at the Max Planck Institute of Biochemistry have deciphered the molecular basis for the chaperone function of clusterin. The researchers were able to determine the crystallographic three-dimensional structure of human clusterin for the first time and discovered that two disordered, hydrophobic peptide tails are crucial for the diverse binding and protective functions of clusterin. The findings have now been published in the journal Nature Structural and Molecular Biology.