Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein

ConclusionsαB-crystallin is capable of distinguishing between aggregation-prone and function-preserving variants, and recognizing the transient unfolding or minor conformers that lead to aggregation in the disease-related variant.General significanceHuman αB-crystallin distinguishes between highly similar variants of a structural crystallin, binding the cataract-related γS-G18V variant, but not the function-preserving γS-G18A variant, which is monomeric at physiological temperature.

Source: Biochimica et Biophysica Acta (BBA) General Subjects - December 7, 2019 Category: Biochemistry Source Type: research