Dissecting Physical Structure of Calreticulin, an Intrinsically Disordered Ca2+-buffering Chaperone from Endoplasmic Reticulum
Document Type
Article
Publication Date
2018
Keywords
calreticulin, intrinsically disordered protein, moonlighting protein, chaperone, protein–protein interaction, posttranslational modifications
Digital Object Identifier (DOI)
https://doi.org/10.1080/07391102.2017.1330224
Abstract
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?
Yes
Citation / Publisher Attribution
Journal of Biomolecular Structure and Dynamics, v. 36, issue 6, p. 1617-1636
Scholar Commons Citation
Migliaccio, Anna Rita and Uversky, Vladimir N., "Dissecting Physical Structure of Calreticulin, an Intrinsically Disordered Ca2+-buffering Chaperone from Endoplasmic Reticulum" (2018). Molecular Medicine Faculty Publications. 235.
https://digitalcommons.usf.edu/mme_facpub/235
