Calmodulin interacts with androglobin and regulates the nitrite reductase activity.

ABSTRACT: Androglobin (Adgb) was discovered as the fifth mammalian globin, but its structure and function remain elusive. In this study, the heme-binding globin domain of Adgb was expressed and its interaction with calmodulin (CaM) was investigated. The protein structure of Adgb and its complex with CaM were predicted using AlphaFold3 and HDOCK. The circularly permutated globin domain of Adgb was well folded with a heme group, which can interact with CaM via the IQ motif. In experimental studies, two mutants of CaM (G41C and G114C) were constructed and labeled with a fluorescent molecule (fluorescein-5-maleimide) in the N-lobe and C-lobe, respectively. Upon binding to Adgb, a greater fluorescence quenching effect was observed for the labeling of Cys41 in the N-lobe due to energy transfer to t

SUBMITTER: Nie LS 

PROVIDER: S-EPMC11665612 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature