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Mapping human calreticulin regions important for structural stability

Biochim Biophys Acta Proteins Proteom. 2021-08; 
Evaldas Čiplys, Tautvydas Paškevičius, Eimantas Žitkus, Juras Bielskis, Raimundas Ražanskas, Tomas Šneideris, Vytautas Smirnovas, Algirdas Kaupinis, David J Tester, Michael J Ackerman, Peter Højrup, Marek Michalak, Gunnar Houen, Rimantas Slibinskas
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Mutant Libraries … P27797) and its mutants were synthesized by GenScript. The genes were subcloned into yeast expression vector pFGADH under control of ADH1 promoter. DNA manipulations were performed according to standard procedures [24], plasmid constructs were verified by Sanger … Get A Quote

摘要

Calreticulin (CALR) is a highly conserved multifunctional chaperone protein primarily present in the endoplasmic reticulum, where it regulates Ca homeostasis. Recently, CALR has gained special interest for its diverse functions outside the endoplasmic reticulum, including the cell surface and extracellular space. Although high-resolution structures of CALR exist, it has not yet been established how different regions and individual amino acid residues contribute to structural stability of the protein. In the present study, we have identified key residues determining the structural stability of CALR. We used a Saccharomyces cerevisiae expression system to express and purify 50 human CALR mutants, which were analy... More

关键词

Calreticulin, Mutants, Secretion, Structural stability, Thermal stability