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 Calreticulin 3D structures

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Michal Harel, Alexander Berchansky