Calcineurin

From Proteopedia

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spinqualitylabelsall models Human calcineurin regulatory subunit B (magenta) and catalytic subunit A (cyan) complex with Ca+2 (green), Fe +3 (orange) and Zn+2 (grey) ions, 1aui Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights 4 3D structures of calcineurin Function Calcineurin (CN) is a eukaryotic calcium-dependent serine/threonine protein phosphatase 2B which dephosphorylates serine/threonine residues. CN activates T cells of the immune system. It participates in Ca+2-dependent signal transduction pathways. For more details see Group:MUZIC:Calcineurin. Relevance CN inhibitors are used as drugs in cases of rheumatic diseases, schizophrenia and diabetes. It is inhibited by immunosuppressant drugs like cyclosporine. Structural highlights It contains a and a . There are (molecules of water are shown as red spheres).[1] 3D structures of calcineurin Calcineurin 3D structures

3D structures of calcineurin

Updated on 18-April-2019

1tco – CN subunit A, B + FK-506-binding protein + Ca + Fe + Zn – bovine
1aui - hCN subunit A, B + Ca + Fe + Zn – human
4il1 – CN subunit A, B/calmodulin + Ca – rat
1m63, 1mf8 - hCN + peptidyl-prolyl cis-trans isomerase + cyclosporine + Ca + Fe + Zn
2p6b - hCN subunit A, B + PVIVIT peptide + Ca + Fe + Zn
3ll8 - hCN subunit A, B + AKAP79 peptide + Ca + Fe + Zn
2jog - hCN subunit A + NFAT peptide
5c1v – hCN subunit A residues 2-347 (mutant) + Fe + Zn
2w73, 2jzi - hCN subunit A calmodulin-binding domain + calmodulin + Ca
4f0z – hCN subunit B + African swine protein virus + Ca
4or9, 4ora, 4orb, 4orc – hCN subunit B + serine/threonine protein phosphatase + Ca + Fe + Zn
5b8i – hCN subunit B + serine/threonine protein phosphatase + peptidyl-prolyl cis-trans isomerase + Ca + Fe + Zn
5sve – hCN subunit B + serine/threonine protein phosphatase + NAFTC1 LXVP peptide + Ca + Fe + Zn

References

1. ↑ Kissinger CR, Parge HE, Knighton DR, Lewis CT, Pelletier LA, Tempczyk A, Kalish VJ, Tucker KD, Showalter RE, Moomaw EW, et al.. Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature. 1995 Dec 7;378(6557):641-4. PMID:8524402 doi:http://dx.doi.org/10.1038/378641a0

See Group:MUZIC:Calcineurin.