Abstract

Calcineurin (CaN) is a Ca - and calmodulin (CaM) binding protein first discovered in brain tissue in 1978 and subsequently found in many different tissue types. It is a hetero dimer composed of a large """"""""A"""""""" subunit and a small """"""""B"""""""" subunit. CaN-A is a class 2B protein phosphatase which contains an autoinhibitory region as well as separate domains for CaN-B and CaM binding. The discovery that CaN binds to immunosuppressive drug-immunophilin complexes implicated this enzyme as a central component of the immune response system. Both the A and the B subunits are required for CaN binding to such complexes and it has been shown that the activity of CaN and not other phosphatases in T-cells is inhibited by drug-immunophilin complexes. We wish to do data collection feasibility studies on CaN/imunophilin-drug complexes.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-17
Application #
5222790
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
17
Fiscal Year
1996
Total Cost
Indirect Cost

  Publications

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Hettle, Andrew; Fillo, Alexander; Abe, Kento et al. (2017) Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of ?-1,3-glucan. J Biol Chem 292:16955-16968
Oberthuer, Dominik; Knoška, Juraj; Wiedorn, Max O et al. (2017) Double-flow focused liquid injector for efficient serial femtosecond crystallography. Sci Rep 7:44628

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