Interfaces Between Alpha-helical Integral Membrane Proteins: Characterization, Prediction, and Docking.

ABSTRACT: Protein-protein interaction (PPI) is an essential mechanism by which proteins perform their biological functions. For globular proteins, the molecular characteristics of such interactions have been well analyzed, and many computational tools are available for predicting PPI sites and constructing structural models of the complex. In contrast, little is known about the molecular features of the interaction between integral membrane proteins (IMPs) and few methods exist for constructing structural models of their complexes. Here, we analyze the interfaces from a non-redundant set of complexes of α-helical IMPs whose structures have been determined to a high resolution. We find that the interface is not significantly different from the rest of the surface in terms of average hydrophobicity. H

SUBMITTER: Li B 

PROVIDER: S-EPMC6603304 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature