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J Biomol Struct Dyn. 2018 May;36(6):1617-1636. doi: 10.1080/07391102.2017.1330224. Epub 2017 May 26.

Dissecting physical structure of calreticulin, an intrinsically disordered Ca2+-buffering chaperone from endoplasmic reticulum.

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a Tisch Cancer Institute, Icahn School of Medicine at Mount Sinai (ISMMS) , New York , NY , USA.
b Department of Biomedical and Neuromotorial Sciences , Alma Mater University , Bologna , Italy.
c Department of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute , Morsani College of Medicine, University of South Florida , Tampa , FL , USA.
d Laboratory of New Methods in Biology , Institute for Biological Instrumentation, Russian Academy of Sciences , Pushchino , Moscow Region 142290 , Russia.


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.


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

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