Elucidating the complex membrane binding of a protein with multiple anchoring domains using extHMMM.

ABSTRACT: Membrane binding is a crucial mechanism for many proteins, but understanding the specific interactions between proteins and membranes remains a challenging endeavor. Coagulation factor Va (FVa) is a large protein whose membrane interactions are complicated due to the presence of multiple anchoring domains that individually can bind to lipid membranes. Using molecular dynamics simulations, we investigate the membrane binding of FVa and identify the key mechanisms that govern its interaction with membranes. Our results reveal that FVa can either adopt an upright or a tilted molecular orientation upon membrane binding. We further find that the domain organization of FVa deviates (sometimes significantly) from its crystallographic reference structure, and that the molecular orientation of the

SUBMITTER: Madsen JJ 

PROVIDER: S-EPMC11257402 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature