Structure-based network analysis of an evolved G protein-coupled receptor homodimer interface.

ABSTRACT: Crystallographic structures and experimental assays of human CXC chemokine receptor type 4 (CXCR4) provide strong evidence for the capacity to homodimerize, potentially as a means of allosteric regulation. Even so, how this homodimer forms and its biological significance has yet to be fully characterized. By applying principles from network analysis, sequence-based approaches such as statistical coupling analysis to determine coevolutionary residues, can be used in conjunction with molecular dynamics simulations to identify residues relevant to dimerization. Here, the predominant coevolution sector lies along the observed dimer interface, suggesting functional relevance. Furthermore, coevolution scoring provides a basis for determining significant nodes, termed hubs, in the network formed

SUBMITTER: Nichols SE 

PROVIDER: S-EPMC3690714 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature