The membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions.

ABSTRACT: α Helices are a basic unit of protein secondary structure and therefore the interaction between helices is crucial to understanding tertiary and higher-order folds. Comparing subtle variations in the structural and sequence motifs between membrane and soluble proteins sheds light on the different constraints faced by each environment and elucidates the complex puzzle of membrane protein folding. Here, we demonstrate that membrane and water-soluble helix pairs share a small number of similar folds with various interhelical distances. The composition of the residues that pack at the interface between corresponding motifs shows that hydrophobic residues tend to be more enriched in the water-soluble class of structures and small residues in the transmembrane class. The latter group facilitates

SUBMITTER: Zhang SQ 

PROVIDER: S-EPMC4351763 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature