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Peptide binding specificity of the chaperone calreticulin

Noreen Sandhu1, Karen Duus, Charlotte S Jørgensen

  • 1Department of Autoimmunology, Statens Serum Institut, Artillerivej 5, DK-2300 Copenhagen, Denmark.

Biochimica Et Biophysica Acta
|May 15, 2007
PubMed
Summary

Calreticulin, a molecular chaperone, binds to specific hydrophobic peptide sequences. Its binding is enhanced by peptide length and hydrophobicity, but hindered by hydrophilic residues.

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