NMR resonance assignments of the catalytic domain of human serine/threonine phosphatase calcineurin in unligated and PVIVIT-peptide-bound states.

ABSTRACT: Calcineurin (Cn) is a serine/threonine phosphatase that plays pivotal roles in many physiological processes. In T cell, Cn targets the nuclear factors of activated T-cell (NFATs), transcription factors that activate cytokine genes. Elevated intracellular calclium concentration activates Cn to dephosphorylate multiple serine residues within the NFAT regulatory domain, which triggers joint nuclear translocation of NFAT and Cn. This relies on the interaction between the catalytic domain of Cn (CnA) and the conserved PxIxIT motif. Here, we present the assignment of CnA resonances in unligated form and in complex with a 14-residue peptide containing a PVIVIT sequence that was derived from affinity driven peptide selection based on the conserved PxIxIT motif of NFATs. Although a complete assignm

SUBMITTER: Takeuchi K 

PROVIDER: S-EPMC4352383 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature