Abstract
With remarkable spatial and temporal specificities, peripheral membrane proteins bind to biological membranes. They do this without compromising solubility of the protein, and their binding sites are not easily distinguished. Prototypical peripheral membrane binding sites display a combination of patches of basic and hydrophobic amino acids that are also frequently present on other protein surfaces. The purpose of this contribution is to identify simple but essential components for membrane binding, through structural criteria that distinguish exposed hydrophobes at membrane binding sites from those that are frequently found on any protein surface. We formulate the concepts of protruding hydrophobes and co-insertability and have analysed more than 300 families of proteins that are classified as peripheral membrane binders. We find that this structural motif strongly discriminates the surfaces of membrane-binding and non-binding proteins. Our model constitutes a novel formulation of a structural pattern for membrane recognition and emphasizes the importance of subtle structural properties of hydrophobic membrane binding sites.
Highlights
Biological membranes are ancient and crucial components in the organisation of life
We find that protruding hydrophobes can be used to strongly discriminate protein surfaces involved in membrane binding from those that are not
In pursuit of such general models for membrane recognition, we have formulated the concepts of protruding hydrophobes and co-insertability
Summary
Biological membranes are ancient and crucial components in the organisation of life Do they define the boundaries of cells and organelles, but they are central to a myriad proteinprotein and protein-lipid interactions instrumental in numerous pathways [1,2,3,4,5]. Besides the embedded transmembrane proteins and receptors, a number of soluble proteins interact transiently with the surface of cellular and organellar membranes achieving remarkable spatial and temporal specificities. These proteins (or domains) are referred to as peripheral proteins (or domains) and their membrane-binding site as interfacial binding site or IBS. Many lipid-processing enzymes, endogenous or secreted by pathogens are included in the definition of peripheral proteins
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