Journal
PLOS ONE
Volume 6, Issue 3, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0017886
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Funding
- CNRS, CEA, Grenoble Universite 1
- National Research Agency [ANR-09-PIRI-0021]
- Agence Nationale de la Recherche (ANR) [ANR-09-PIRI-0021] Funding Source: Agence Nationale de la Recherche (ANR)
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In the endoplasmic reticulum, calreticulin acts as a chaperone and a Ca2+-signalling protein. At the cell surface, it mediates numerous important biological effects. The crystal structure of the human calreticulin globular domain was solved at 1.55 angstrom resolution. Interactions of the flexible N-terminal extension with the edge of the lectin site are consistently observed, revealing a hitherto unidentified peptide-binding site. A calreticulin molecular zipper, observed in all crystal lattices, could further extend this site by creating a binding cavity lined by hydrophobic residues. These data thus provide a first structural insight into the lectin-independent binding properties of calreticulin and suggest new working hypotheses, including that of a multi-molecular mechanism.
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