3POW
Crystal structure of the globular domain of human calreticulin
Summary for 3POW
| Entry DOI | 10.2210/pdb3pow/pdb |
| Related | 3POS |
| Descriptor | calreticulin, CALCIUM ION (3 entities in total) |
| Functional Keywords | legume lectin fold, cnx/crt family, multi-functional, carbohydrate binding, peptide binding, multi-compartmental, chaperone |
| Biological source | Homo sapiens (human) More |
| Cellular location | Endoplasmic reticulum lumen : P27797 |
| Total number of polymer chains | 1 |
| Total formula weight | 30186.35 |
| Authors | Gaboriaud, C. (deposition date: 2010-11-23, release date: 2011-03-09, Last modification date: 2024-10-30) |
| 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 Cited by 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: 21423620DOI: 10.1371/journal.pone.0017886 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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