The conformational plasticity of structurally unrelated lipid transport proteins correlates with their mode of action.

ABSTRACT: Lipid transfer proteins (LTPs) are key players in cellular homeostasis and regulation, as they coordinate the exchange of lipids between different cellular organelles. Despite their importance, our mechanistic understanding of how LTPs function at the molecular level is still in its infancy, mostly due to the large number of existing LTPs and to the low degree of conservation at the sequence and structural level. In this work, we use molecular simulations to characterize a representative dataset of lipid transport domains (LTDs) of 12 LTPs that belong to 8 distinct families. We find that despite no sequence homology nor structural conservation, the conformational landscape of LTDs displays common features, characterized by the presence of at least 2 main conformations whose populations are

SUBMITTER: Srinivasan S 

PROVIDER: S-EPMC11361750 | biostudies-literature | 2024 Aug

REPOSITORIES: biostudies-literature