Influence of oligomerization on the dynamics of G-protein coupled receptors as assessed by normal mode analysis

Masha Y. Niv, Marta Filizola*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


The recently discovered impact of oligomerization on G-protein coupled receptor (GPCR) function further complicates the already challenging goal of unraveling the molecular and dynamic mechanisms of these receptors. To help understand the effect of oligomerization on the dynamics of GPCRs, we have compared the motion of monomeric, dimeric, and tetrameric arrangements of the prototypic GPCR rhodopsin, using an approximate - yet powerful - normal mode analysis (NMA) technique termed elastic network model (ENM). Moreover, we have used ENM to discriminate between putative dynamic mechanisms likely to account for the recently observed conformational rearrangement of the TM4,5-TM4,5 dimerization interface of GPCRs that occurs upon activation. Our results indicate: (1) significant perturbation of the normal modes (NMs) of the rhodopsin monomer upon oligomerization, which is mainly manifested at interfacial regions; (2) increased positive correlation among the transmembrane domains (TMs) and between the extracellular loop (EL) and TM regions of the rhodopsin protomer; (3) highest interresidue positive correlation at the interfaces between protomers; and (4) experimentally testable hypotheses of differential motional changes within different putative oligomeric arrangements.

Original languageAmerican English
Pages (from-to)575-586
Number of pages12
JournalProteins: Structure, Function and Genetics
Issue number2
StatePublished - 1 May 2008


  • Activation
  • Coarse grained
  • Complexation
  • Correlation
  • Dimerization
  • Elastic network model
  • GPCRs
  • Interface
  • Rhodopsin


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