Calcineurin
From Proteopedia
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| - | {{STRUCTURE_1aui| PDB=1aui | SIZE=400| SCENE= |right|CAPTION=Human calcineurin subunit | + | {{STRUCTURE_1aui| PDB=1aui | SIZE=400| SCENE= |right|CAPTION=Human calcineurin regulatory subunit B (green) and catalytic subunit A (grey) complex with Ca+2 (green), Fe +3 (red) and Zn+2 (grey) ions, [[1aui]] }} |
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== Structural highlights == | == Structural highlights == | ||
| - | It contains a calmodulin-binding catalytic subunit and a Ca+2-binding regulatory subunit. There are 2 metal ions in CN active site. | + | It contains a calmodulin-binding catalytic subunit A and a Ca+2-binding regulatory subunit B. There are 2 metal ions in CN active site. |
==3D structures of calcineurin== | ==3D structures of calcineurin== | ||
Revision as of 10:34, 16 November 2015
Contents |
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 calmodulin-binding catalytic subunit A and a Ca+2-binding regulatory subunit B. There are 2 metal ions in CN active site.
3D structures of calcineurin
Updated on 16-November-2015
1tco – CN + FK-506-binding protein + Ca + Fe + Zn – bovine
1aui - hCN + Ca + Fe + Zn – human
4il1 – CN + Ca – rat
1m63, 1mf8 - hCN + peptidyl-prolyl cis-trans isomerase + cyclosporine + Ca + Fe + Zn
2p6b - hCN + PVIVIT peptide + Ca + Fe + Zn
3ll8 - hCN + AKAP79 peptide + Ca + Fe + Zn
2jog - hCN catalytic subunit + NFAT peptide
2jzi - hCN catalytic subunit + calmodulin + Ca
2w73 - hCN calmodulin-binding domain + calmodulin + Ca
4f0z – hCN subunit B + African swine protein virus + Ca
