ArticleProteins2008
Influence of oligomerization on the dynamics of G-protein coupled receptors as assessed by normal mode analysis.
Article in Proteins, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Dynamic properties of oligomers that characterize low-frequency normal modes.Biophysics and physicobiology · 2019Article
- Normal mode analysis as a method to derive protein dynamics information from the Protein Data Bank.Biophysical reviews · 2017Review
- Genome-wide Membrane Protein Structure Prediction.Current genomics · 2013Article
- Elastic Network Models are Robust to Variations in Formalism.Journal of chemical theory and computation · 2012Article
- Changes in dynamics upon oligomerization regulate substrate binding and allostery in amino acid kinase family members.PLoS computational biology · 2011Article
- Increasingly accurate dynamic molecular models of G-protein coupled receptor oligomers: Panacea or Pandora's box for novel drug discovery?Life sciences · 2010Review
- Asymmetric conformational flexibility in the ATP-binding cassette transporter HI1470/1.Biophysical journal · 2009Article
- Progress in elucidating the structural and dynamic character of G Protein-Coupled Receptor oligomers for use in drug discovery.Current pharmaceutical design · 2009Review
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Authors and funding
2 authors.
Funding
Abstract
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.
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Registered trials
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