The Recognition of Calmodulin to the Target Sequence of Calcineurin-A Novel Binding Mode.

ABSTRACT: Calcineurin (CaN) is a Ca²⁺/calmodulin-dependent Ser/Thr protein phosphatase, which plays essential roles in many cellular and developmental processes. CaN comprises two subunits, a catalytic subunit (CaN-A, 60 kDa) and a regulatory subunit (CaN-B, 19 kDa). CaN-A tightly binds to CaN-B in the presence of minimal levels of Ca²⁺, but the enzyme is inactive until activated by CaM. Upon binding to CaM, CaN then undergoes a conformational rearrangement, the auto inhibitory domain is displaced and thus allows for full activity. In order to elucidate the regulatory role of CaM in the activation processes of CaN, we used NMR spectroscopy to determine the structure of the complex of CaM and the target peptide of CaN (CaNp). The CaM/CaNp complex shows a compact ellipsoidal shap

SUBMITTER: Chyan CL 

PROVIDER: S-EPMC6151454 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature