Title : Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin.

Pub. Date : 2006 Jan 27

PMID : 16291754






1 Functional Relationships(s)
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1 We have focused on two cysteine residues (Cys(88) and Cys(120)), which form a disulfide bridge in the N-terminal domain of calreticulin, on a tryptophan residue located in the carbohydrate binding site (Trp(302)), and on certain residues located at the tip of the "hairpin-like" P-domain of the protein (Glu(238), Glu(239), Asp(241), Glu(243), and Trp(244)). Carbohydrates calreticulin Homo sapiens