Sulfur-containing amino acids in 7TMRs: Molecular gears for pharmacology and function

Arnau Cordomí, José C. Gómez-Tamayo, Véronique Gigoux, Daniel Fourmy

Research output: Contribution to journalReview articleResearchpeer-review

21 Citations (Scopus)


Seven-transmembrane receptors (7TMRs) mediate the majority of physiological responses to hormones and neurotransmitters in higher organisms. Tertiary structure stability and activation of these versatile membrane proteins require formation or disruption of complex networks of well-recognized interactions (such as H-bonds, ionic, or aromatic-aromatic) but also of other type of interactions which have been less studied. In this review, we compile evidence from crystal structure, biophysical, and site-directed mutagenesis data that indicate or support the importance of interactions involving Met and Cys in 7TMRs in terms of pharmacology and function. We show examples of Met/Cys-aromatic and Met-Met interactions participating in ligand binding, in tuning the orientation of functionally important aromatic residues during activation or even in modulating the type of signaling response. Collectively, data presented enlarge the repertoire of interactions governing 7TMR functioning. © 2013 Published by Elsevier Ltd.
Original languageEnglish
Pages (from-to)320-331
JournalTrends in Pharmacological Sciences
Issue number6
Publication statusPublished - 1 Jun 2013


  • crystal structure
  • GPCR
  • molecular modeling
  • site-directed mutagenesis


Dive into the research topics of 'Sulfur-containing amino acids in 7TMRs: Molecular gears for pharmacology and function'. Together they form a unique fingerprint.

Cite this