The cooperative folding of annexin A2 relies on a transient nonnative intermediate.

ABSTRACT: Annexins (Anxs) are a family of highly homologous proteins that bind and aggregate lipid vesicles in the presence of calcium. All members of the family contain a variable N-terminus determining specific functions, followed by a conserved core region responsible for the general calcium-dependent lipid-binding property. The core structure consists of four homologous domains (D_I-D_IV), each consisting of a right-handed super-helix of five α-helices. We present data from a combination of site-directed mutagenesis, NMR, and circular dichroism showing that the G25-D34 region of the N-terminus as well as the contacts between residues D38A, R63A, and Q67A of AnxA2-D_I are crucial for the autonomous folding and stability of D_I of AnxA2. However, we also sho

SUBMITTER: Hollas H 

PROVIDER: S-EPMC9748365 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature