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1aui

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{{STRUCTURE_1aui| PDB=1aui | SCENE= }}
{{STRUCTURE_1aui| PDB=1aui | SCENE= }}
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'''HUMAN CALCINEURIN HETERODIMER'''
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===HUMAN CALCINEURIN HETERODIMER===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8524402 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8524402}}
==About this Structure==
==About this Structure==
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[[Category: Immunosuppression]]
[[Category: Immunosuppression]]
[[Category: Phosphatase]]
[[Category: Phosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:42:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:37:03 2008''

Revision as of 14:37, 30 June 2008

Image:1aui.png

Template:STRUCTURE 1aui

HUMAN CALCINEURIN HETERODIMER

Template:ABSTRACT PUBMED 8524402

About this Structure

1AUI is a Protein complex structure of sequences from Homo sapiens. 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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