Fractal dimension as a measure of surface roughness of G protein-coupled receptors: implications for structure and function.

ABSTRACT: Protein surface roughness is a structural property associated with ligand-protein and protein-protein binding interfaces. In this work we apply for the first time the concept of surface roughness, expressed as the fractal dimension, to address structure and function of G protein-coupled receptors (GPCRs) which are an important group of drug targets. We calculate the exposure ratio and the fractal dimension for helix-forming residues of the β(2) adrenergic receptor (β(2)AR), a model system in GPCR studies, in different conformational states: in complex with agonist, antagonist and partial inverse agonists. We show that both exposure ratio and roughness exhibit periodicity which results from the helical structure of GPCRs. The pattern of roughness and exposure ratio of a protein patch depend

SUBMITTER: Kaczor AA 

PROVIDER: S-EPMC3429779 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature