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

Ca-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).

Modeling the Annexin A1-S100A11 heterotetramer: a molecular dynamics investigation of structure and correlated motion.

Annexin A1 (A1) has been shown to form a tetrameric complex (A1t) with S100A11 which is implicated in calcium homeostasis and EGFR pathways. In this work, a full-length model of the A1t was generated for the first time. Multiple molecular dynamics simulations were performed on the complete A1t model for several hundred nanoseconds each to assess the structure and dynamics of A1t.

Ca ions facilitate the organization of the Annexin A2/S100A10 heterotetramer.

Annexin A2 (A2) is a member of the Annexin family, which contains Ca -regulated phospholipid-binding proteins. Annexins associate with S100 proteins to form heterotetramers. The A2/S100A10 heterotetramer (A2t) is the most extensively studied of these heterotetramers.

Nudged Elastic Band Study on the N-Terminal Domain Conformational Pathways of Annexin A1 from a Buried State to an Exposed State.

Mapping the conformational pathway of biomolecules is a great challenge because of the large size and complexity of biomolecules. The nudged elastic band (NEB) method has been applied to study the reaction pathways for both small organic molecules and small peptides of a few amino acids. In this work, for the first time, the NEB method was employed to study the conformational pathways of Annexin A1, a membrane-binding protein of 334 amino acids.