3POS

Crystal structure of the globular domain of human calreticulin

Summary for 3POS

• Entry DOI: 10.2210/pdb3pos/pdb
• Related: 3POW
• Descriptor: Calreticulin, CALCIUM ION (3 entities in total)
• Functional Keywords: legume lectin fold, cnx/crt family, multi-functional, chaperone, carbohydrate binding, peptide binding, multi-compartmental
• Biological source: Homo sapiens (human); More
• Cellular location: Endoplasmic reticulum lumen : P27797
• Total number of polymer chains: 3
• Total formula weight: 90559.05

Authors

Chouquet, A.,Paidassi, H.,Ling, W.-L.,Frachet, P.,Houen, G.,Arlaud, G.J.,Gaboriaud, C. (deposition date: 2010-11-23, release date: 2011-03-09, Last modification date: 2024-10-16)

Primary citation

Chouquet, A.,Paidassi, H.,Ling, W.L.,Frachet, P.,Houen, G.,Arlaud, G.J.,Gaboriaud, C.
X-ray structure of the human calreticulin globular domain reveals a Peptide-binding area and suggests a multi-molecular mechanism
Plos One, 6:e17886-e17886, 2011

PubMed Abstract: 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 Å 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.

PubMed: 21423620
DOI: 10.1371/journal.pone.0017886

Experimental method

X-RAY DIFFRACTION (1.65 Å)