Background: Human alphaB crystallin (HspB5) contains the alpha crystallin core domain, a series of antiparallel beta-strands organized into the characteristic beta sandwich of small heat shock proteins (sHsps). The full 3-dimensional structure for alpha crystallin has not been determined and the mechanism for the biological activity remains elusive because sHsps participate in multiple interactions with a broad range of target proteins that favor self-assembly of polydisperse fibrils and complexes. We selected human alphaB crystallin to study interactive sequences because it is involved in many human condensation, amyloid, and aggregation diseases and it is very sensitive to the destabilization of unfolding proteins. Sophisticated methods are being used to analyze and complete the structure of alphaB crystallin with the expectation of understanding sHsp function. This review considers the identification of interactive sites on the surface of the alphaB crystallin, which may be the key to understanding the multifunctional activity of human alphaB crystallin.
Scope of review: This review summarizes the research on the identification of the bioactive interactive sequences responsible for the function of human alphaB crystallin, an sHsp with chaperone-like activity.
Major conclusions: The multifunctional activity of human alphaB crystallin results from the interactive peptide sequences exposed on the surface of the molecule. The multiple, non-covalent, interactive sequences can account for the selectivity and sensitivity of alphaB crystallin to the initiation of protein unfolding.
General significance: Human alphaB crystallin may be an important part of an endogenous protective mechanism in aging cells and tissues. This article is part of a Special Issue entitled Crystallin Biochemistry in Health and Disease.
Keywords: Amyloid; Cataract; Crystallin; Human; Lens; Pin array.
Copyright © 2015. Published by Elsevier B.V.