Interactions and conformational changes of annexin A2/p11 heterotetramer models on a membrane: a molecular dynamics study.

ABSTRACT: Ca²⁺-dependent membrane-binding by the Annexin A2/p11 heterotetramer (A2t) plays an important role in various biological processes including fibrinogen activation and exocytosis in neuroendocrine cells. Two models where A2t associates with a single membrane surface were generated and used to perform molecular dynamics simulations. The first model mimics initial A2t-membrane binding through both Annexin A2 (A2) subunits of A2t (TS model) while the second model mimics A2t-binding through a single A2 subunit (OS model). Conformational changes were summarized using principal component analysis (PCA), simulation snapshots, and distance plots from the simulations. The full TS model, including the p11 dimer, fully associates with the membrane adopting a stable structure with little con

SUBMITTER: Lindsay S 

PROVIDER: S-EPMC11611455 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature