Picosecond Dynamics of the Glutamate Receptor in Response to Agonist-Induced Vibrational Excitation

Minoru Kubo, Eiji Shiomitsu, Kei Odai, Tohru Sugimoto, Hideo Suzuki, Etsuro Ito*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


Conformational changes of proteins are dominated by the excitation and relaxation processes of their vibrational states. To elucidate the mechanism of receptor activation, the conformation dynamics of receptors must be analyzed. in response to agonist-induced vibrational excitation. In this study, we chose the bending vibrational mode of the guanidinium group of Arg485 of the glutamate receptor subunit GluR2 based on our previous studies, and we investigated picosecond dynamics of the glutamate receptor caused by the vibrational excitation of Arg485 via molecular dynamics simulations. The vibrational excitation energy in Arg485 in the ligand-binding site initially flowed into Lys730, and then into the J-helix at the subunit interface of the ligand-binding domain. Consequently, the atomic displacement in the subunit interface around an intersubunit hydrogen bond was evoked in about 3 ps. This atomic displacement may perturb the subunit packing of the receptor, triggering receptor activation.

Original languageEnglish
Pages (from-to)231-236
Number of pages6
JournalProteins: Structure, Function and Genetics
Issue number2
Publication statusPublished - 2004 Feb 1
Externally publishedYes


  • Conformational change
  • Energy transfer
  • Ionotropic receptor
  • Molecular dynamics simulation
  • Receptor activation

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology


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