Lipid recognition propensities of amino acids in membrane proteins from atomic resolution data.

ABSTRACT:

Background

Protein-lipid interactions play essential roles in the conformational stability and biological functions of membrane proteins. However, few of the previous computational studies have taken into account the atomic details of protein-lipid interactions explicitly.

Results

To gain an insight into the molecular mechanisms of the recognition of lipid molecules by membrane proteins, we investigated amino acid propensities in membrane proteins for interacting with the head and tail groups of lipid molecules. We observed a common pattern of lipid tail-amino acid interactions in two different data sources, crystal structures and molecular dynamics simulations. These interactions are largely explained by general lipophilicity, whereas the preferences for lipid head groups v

SUBMITTER: Morita M 

PROVIDER: S-EPMC3747235 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature