1aui

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[[Image:1aui.gif|left|200px]]<br />
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[[Image:1aui.jpg|left|200px]]<br /><applet load="1aui" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1aui" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1aui, resolution 2.1&Aring;" />
caption="1aui, resolution 2.1&Aring;" />
'''HUMAN CALCINEURIN HETERODIMER'''<br />
'''HUMAN CALCINEURIN HETERODIMER'''<br />
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==About this Structure==
==About this Structure==
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1AUI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, ZN and FE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Structure known Active Sites: CA1, CA2, CA3, CA4, FEB and ZNB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AUI OCA].
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1AUI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, ZN and FE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Known structural/functional Sites: <scene name='pdbsite=CA1:Ca Binding Site'>CA1</scene>, <scene name='pdbsite=CA2:Ca Binding Site'>CA2</scene>, <scene name='pdbsite=CA3:Ca Binding Site'>CA3</scene>, <scene name='pdbsite=CA4:Ca Binding Site'>CA4</scene>, <scene name='pdbsite=FEB:Fe Binding Site'>FEB</scene> and <scene name='pdbsite=ZNB:Zn Binding Site'>ZNB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AUI OCA].
==Reference==
==Reference==
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[[Category: phosphatase]]
[[Category: phosphatase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:02:15 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:21:34 2007''

Revision as of 12:11, 18 December 2007


1aui, resolution 2.1Å

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HUMAN CALCINEURIN HETERODIMER

Contents

Overview

Calcineurin (CaN) is a calcium- and calmodulin-dependent protein, serine/threonine phosphate which is critical for several important, cellular processes, including T-cell activation. CaN is the target of the, immunosuppressive drugs cyclosporin A and FK506, which inhibit CaN after, forming complexes with cytoplasmic binding proteins (cyclophilin and, FKBP12, respectively). We report here the crystal structures of, full-length human CaN at 2.1 A resolution and of the complex of human CaN, with FKBP12-FK506 at 3.5 A resolution. In the native CaN structure, an, auto-inhibitory element binds at the Zn/Fe-containing active site. The, metal-site geometry and active-site water structure suggest a catalytic, mechanism involving nucleophilic attack on the substrate phosphate by a, metal-activated water molecule. In the FKBP12-FK506-CaN complex, the, auto-inhibitory element is displaced from the active site. The site of, binding of FKBP12-FK506 appears to be shared by other non-competitive, inhibitors of calcineurin, including a natural anchoring protein.

Disease

Known diseases associated with this structure: Cornea plana congenita, recessive OMIM:[603288], Myotonic dystrophy, type 2 OMIM:[116955]

About this Structure

1AUI is a Protein complex structure of sequences from Homo sapiens with CA, ZN and FE as ligands. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Known structural/functional Sites: , , , , and . Full crystallographic information is available from OCA.

Reference

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

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