Discrete structural features among interface residue-level classes.

ABSTRACT:

Background

Protein-protein interaction (PPI) is essential for molecular functions in biological cells. Investigation on protein interfaces of known complexes is an important step towards deciphering the driving forces of PPIs. Each PPI complex is specific, sensitive and selective to binding. Therefore, we have estimated the relative difference in percentage of polar residues between surface and the interface for each complex in a non-redundant heterodimer dataset of 278 complexes to understand the predominant forces driving binding.

Results

Our analysis showed ~60% of protein complexes with surface polarity greater than interface polarity (designated as class A). However, a considerable number of complexes (~40%) have interface polarity greater than surface polarity, (design

SUBMITTER: Sowmya G 

PROVIDER: S-EPMC4682381 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature