Calreticulin

spinqualitylabelsall models Human calreticulin (gold) complex withβ-microglobulin (green), tapasin (pink), protein disulfide-isomerase (yellow) MHC class I antigen (cyan) (PDB code 6eny) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Calreticulin (CALR) is a multifunction calcium-binding chaperone. CALR is a molecular chaperone, an extracellular lectin, an intracellular mediator of integrin function, an inhibitor of steroid hormone-regulated gene expression and a C1q-binding protein. Disease Most patients with essential thrombocythemia or primary myelofibrosis not associated with JAK2 or MPL mutation have CALR mutation. Relevance CALR is active in regulating intracellular Ca+2 homeostasis. Structural highlights CALR structure consists of 3 domains: N-terminal globular domain which has chaperone function; P-domain which is proline-rich, binds Ca+2 with high affinity and possesses a lectin-like chaperone function; C-terminal domain containing an ER retention signal.

3D Structures of calreticulin

Updated on 29-January-2018

1hhn, 1k91, 1k9c – CALR P domain 189-288 – rat - NMR
6eny – hCALR + β-microglobulin + tapasin + protein disulfide-isomerase + MHC class I antigen – human
5v90 – hCALR P domain 238-273 + ERP29
3o0v, 3o0w, 3o0x, 3rg0 – CALR lectin domain 18-206 301-368 (mutant) – mouse
3pos, 3pow – hCALR lectin domain 18-206 301-368
5lk5 – hCALR lectin domain 18-206 301-368 (mutant)
5hca, 5hcb – CALR lectin domain 18-206 301-368 + glucose – Entamoeba histolytica

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky