Structural highlights
Publication Abstract from PubMed
In the endoplasmic reticulum, calreticulin acts as a chaperone and a Ca(2+)-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 A 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.
X-ray structure of the human calreticulin globular domain reveals a Peptide-binding area and suggests a multi-molecular mechanism.,Chouquet A, Paidassi H, Ling WL, Frachet P, Houen G, Arlaud GJ, Gaboriaud C PLoS One. 2011 Mar 15;6(3):e17886. PMID:21423620[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chouquet A, Paidassi H, Ling WL, Frachet P, Houen G, Arlaud GJ, Gaboriaud C. X-ray structure of the human calreticulin globular domain reveals a Peptide-binding area and suggests a multi-molecular mechanism. PLoS One. 2011 Mar 15;6(3):e17886. PMID:21423620 doi:10.1371/journal.pone.0017886
