Crystal structures of human calcineurin and the human FKBP12–FK506–calcineurin complex View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-12

AUTHORS

Charles R. Kissinger, Hans E. Parge, Daniel R. Knighton, Cristina T. Lewis, Laura A. Pelletier, Anna Tempczyk, Vincent J. Kalish, Kathleen D. Tucker, Richard E. Showalter, Ellen W. Moomaw, Louis N. Gastinel, Noriyuki Habuka, Xinghai Chen, Fausto Maldonado, John E. Barker, Russell Bacquet, J. Ernest Villafranca

ABSTRACT

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. More... »

PAGES

641-644

Journal

TITLE

Nature

ISSUE

6557

VOLUME

378

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/378641a0

DOI

http://dx.doi.org/10.1038/378641a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1018812919

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8524402


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