Dissecting Physical Structure of Calreticulin, an Intrinsically Disordered Ca2+-buffering Chaperone from Endoplasmic Reticulum

Document Type


Publication Date



calreticulin, intrinsically disordered protein, moonlighting protein, chaperone, protein–protein interaction, posttranslational modifications

Digital Object Identifier (DOI)



Calreticulin (CALR) is a Ca2+ binding multifunctional protein that mostly resides in the endoplasmic reticulum (ER) and plays a number of important roles in various physiological and pathological processes. Although the major functions ascribed to CALR are controlling the Ca2+ homeostasis in ER and acting as a lectin-like ER chaperon for many glycoproteins, this moonlighting protein can be found in various cellular compartments where it has many non-ER functions. To shed more light on the mechanisms underlying polyfunctionality of this moonlighting protein that can be found in different cellular compartments and that possesses a wide spectrum of unrelated biological activities, being able to interact with Ca2+ (and potentially other metal ions), RNA, oligosaccharides, and numerous proteins, we used a set of experimental and computational tools to evaluate the intrinsic disorder status of CALR and the role of calcium binding on structural properties and conformational stability of the full-length CALR and its isolated P- and C-domains.

Was this content written or created while at USF?


Citation / Publisher Attribution

Journal of Biomolecular Structure and Dynamics, v. 36, issue 6, p. 1617-1636