Lessons from Free Energy Simulations of δ-Opioid Receptor Homodimers Involving the Fourth Transmembrane Helix | Zendy

Davide Provasi | Zendy; Jennifer M. Johnston | Zendy; Marta Filizola | Zendy

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Lessons from Free Energy Simulations of δ-Opioid Receptor Homodimers Involving the Fourth Transmembrane Helix

Author(s) -

Davide Provasi,

Jennifer M. Johnston,

Marta Filizola

Publication year - 2010

Publication title -

biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.43

H-Index - 253

eISSN - 1520-4995

pISSN - 0006-2960

DOI - 10.1021/bi100686t

Subject(s) - transmembrane domain , g protein coupled receptor , transmembrane protein , umbrella sampling , helix (gastropod) , receptor , membrane , chemistry , lipid bilayer , biophysics , opioid receptor , molecular dynamics , biology , biochemistry , opioid , computational chemistry , ecology , snail

Several G protein-coupled receptors (GPCRs), including opioid receptors deltaOR, muOR, and kappaOR, have been reported to form stable dimers or oligomers in lipid bilayers and cell membranes. This notion has been recently challenged by imaging data supporting a transient nature of GPCR association. Here we use umbrella sampling reconstructed free energies of deltaOR homodimers involving the fourth transmembrane helix to predict their association constant. The results of these simulations, combined with estimates of diffusion-limited association rates, suggest a short lifetime for deltaOR homodimers in the membrane, in agreement with recent trends.

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