Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin*

HIGHLIGHTS

• who: Virginie Martin from the ticulinThus, it appears that clusters of negatively charged residues at the tip of the, domain, in both calreticulin and calnexin, play an important role in promoting and stabilizing association with ERp57. In conclusion, a number of cell biological, molecular, and biophysical studies have been used to identify functionally important regions and amino acid residues in calreticulin (12) (this study). Certain amino acid residues located directly in (Trp302) or near (His153) (12) the carbohydrate pocket are critical for the chaperone function of the protein. Further, modification of a residue(s) in the carbohydrate . . .
  

   

  

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