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

Catch Bond-Mediated Adhesion Drives Staphylococcus aureus Host Cell Invasion

“…The N-terminal domain is a variable, intrinsically disordered region that contains sites for post-translation modifications including acetylation, serine/tyrosine phosphorylation, and for binding to S100A10, a protein that forms heterotetramers with annexin A2. The conserved C-terminal core domain is composed of four homologous repeats of about 70 amino acids, each consisting of a right-handed superhelix of five α-helices . The core domain interacts with calcium and with many biomolecules, including RNA, − phospholipids, − heparin, and F-actin. , …”

“…The conserved C-terminal core domain is composed of four homologous repeats of about 70 amino acids, each consisting of a right-handed superhelix of five α-helices. 5 The core domain interacts with calcium 6 and with many biomolecules, including RNA, 7−9 phospholipids, 10−12 heparin, 13 and F-actin. 10,14 Viruses 15 and pathogenic bacteria 16 interact with surfaceexposed annexin A2 to favor colonization and invasion of host cells.…”