Calcineurin

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:43, 6 February 2022) (edit) (undo)
 
(23 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_1aui| PDB=2p6b | SIZE=400| SCENE= |right|CAPTION=Human calcineurin subunit β (yellow and green) and calmodulin-dependent calcineurin subunit α (grey and pink) complex with polypeptide (magenta), phosphate, Ca+2 (green), Fe +3 and Zn+2 (grey) ions, [[1aui]] }}
+
<StructureSection load='1aui' size='350' side='right' scene='48/489261/Cv/1' caption='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]]'>
 +
== 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.
-
Please use the "3D" button above this box to insert a Jmol applet (molecule) on this page.
+
For more details see [[Group:MUZIC:Calcineurin]].
-
Or use the four-green-boxes-button to insert scrollable text adjacent
+
-
to a Jmol applet. Check out the other buttons as well!
+
-
-->
+
-
'''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. It contains a calmodulin-binding catalytic subunit and a Ca+2-binding regulatory subunit. There are 2 metal ions in CN active site. CN inhibitors are used as drugs in cases of rheumatic diseases, schizophrenia and diabetes. It is inhibited by immunosuppressant drugs like cyclosporine. For more details see [[Group:MUZIC:Calcineurin]].
+
-
==3D structures of calcineurin==
+
== Relevance ==
-
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+
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 <scene name='48/489261/Cv/2'>calmodulin-binding catalytic subunit A</scene> and a <scene name='48/489261/Cv/3'>Ca+2-binding regulatory subunit B</scene>. There are <scene name='48/489261/Cv/5'>2 metal ions in CN active site</scene> (molecules of water are shown as red spheres).<ref>PMID:8524402</ref>
 +
 
 +
==3D structures of calcineurin==
 +
[[Calcineurin 3D structures]]
-
[[1tco]] – CN + FK-506-binding protein + Ca + Fe + Zn – bovine<br />
+
-
[[1aui]] - hCN + Ca + Fe + Zn – human<br />
+
</StructureSection>
-
[[1m63]], [[1mf8]] - hCN + peptidyl-prolyl cis-trans isomerase + cyclosporine + Ca + Fe + Zn<br />
+
-
[[2p6b]] - hCN + PVIVIT peptide + Ca + Fe + Zn<br />
+
-
[[3ll8]] - hCN + AKAP79 peptide + Ca + Fe + Zn<br />
+
-
[[2jog]] - hCN catalytic subunit + NFAT peptide<br />
+
-
[[2jzi]] - hCN catalytic subunit + calmodulin + Ca <br />
+
-
[[2w73]] - hCN calmodulin-binding domain + calmodulin + Ca
+
 +
==References==
 +
<references/>
 +
See [[Group:MUZIC:Calcineurin]].
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate

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.

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Calcineurin"
Personal tools