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- W2014223927 endingPage "1674" @default.
- W2014223927 startingPage "1659" @default.
- W2014223927 abstract "Calcineurin is a phosphoprotein phosphatase that channels intracellular Ca signals into multiple biological pathways. Calcineurin is known to interact directly with its substrate nuclear factor of activated T cells (NFAT or NFATc), with other substrates, and with several targeting and scaffold proteins including AKAP79 and Cabin1/cain. The calcineurin-NFAT interaction depends on recognition of a PxIxIT sequence motif present in NFAT-family proteins and in certain other calcineurin-interacting proteins. Here, we define the structural basis for the interaction of calcineurin with NFAT and with other proteins possessing the PxIxIT motif. The calcineurin-PxIxIT contact has a direct parallel in the contact of protein phosphatase 1 with its regulatory proteins, suggesting that the evolution of these related phosphatases involved local remodelling of an ancestral docking site." @default.
- W2014223927 created "2016-06-24" @default.
- W2014223927 creator A5002370058 @default.
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- W2014223927 date "2004-10-01" @default.
- W2014223927 modified "2023-10-17" @default.
- W2014223927 title "Structural Delineation of the Calcineurin–NFAT Interaction and its Parallels to PP1 Targeting Interactions" @default.
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- W2014223927 doi "https://doi.org/10.1016/j.jmb.2004.07.068" @default.
- W2014223927 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15364589" @default.
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