NDLI: Crystal structure of calcineurin–cyclophilin–cyclosporin shows common but distinct recognition of immunophilin

Content Provider	PubMed Central
Author	Qing, Huai Kim, Hwa-young Liu, Yudong Zhao, Yingdong Mondragon, Angelo Liu, Jun O. Ke, Hengming
Copyright Year	2002
Abstract	Calcineurin, a Ca2+/calmodulin-dependent protein phosphatase, is the common target for two immunophilin–immunosuppressant complexes, cyclophilin A–cyclosporin A (CyPA-CsA) and FKBP–FK506. How the two structurally distinct immunophilin–drug complexes bind the same target has remained unknown. We report the crystal structure of calcineurin (CN) in complex with CyPA-CsA at 2.8-Å resolution. The CyPA-CsA complex binds to a composite surface formed by the catalytic and regulatory subunits of CN, where the complex of FK506 and its binding protein FKBP also binds. While the majority of the CN residues involved in the binding are common for both immunophilin-immunosuppressant complexes, a significant number of the residues are distinct. Unlike FKBP-FK506, CyPA-CsA interacts with Arg-122 at the active site of CN, implying direct involvement of CyPA-CsA in the regulation of CN catalysis. The simultaneous interaction of CyPA with both the composite surface and the active site of CN suggests that the composite surface may serve as a substrate recognition site responsible for the narrow substrate specificity of CN. The comparison of CyPA-CsA-CN with FKBP-FK506-CN significantly contributes to understanding the molecular basis of regulation of CN activity by the immunophilin–immunosuppressant.
Related Links	http://dx.doi.org/10.1073/pnas.192206699
Ending Page	12042
Page Count	6
Starting Page	12037
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	19
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-09-17
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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