6BE1

Cryo-EM structure of serotonin receptor

Summary for 6BE1

• Entry DOI: 10.2210/pdb6be1/pdb
• EMDB information: 7088
• Descriptor: 5-hydroxytryptamine receptor 3A, beta-D-mannopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
• Functional Keywords: ion channel, membrane protein
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 5
• Total formula weight: 274179.97

Authors

Basak, S.,Chakrapani, S. (deposition date: 2017-10-24, release date: 2018-02-07, Last modification date: 2024-10-23)

Primary citation

Basak, S.,Gicheru, Y.,Samanta, A.,Molugu, S.K.,Huang, W.,Fuente, M.,Hughes, T.,Taylor, D.J.,Nieman, M.T.,Moiseenkova-Bell, V.,Chakrapani, S.
Cryo-EM structure of 5-HT
Nat Commun, 9:514-514, 2018

PubMed Abstract: Serotonin receptors (5-HTR) directly regulate gut movement, and drugs that inhibit 5-HTR function are used to control emetic reflexes associated with gastrointestinal pathologies and cancer therapies. The 5-HTR function involves a finely tuned orchestration of three domain movements that include the ligand-binding domain, the pore domain, and the intracellular domain. Here, we present the structure from the full-length 5-HTR channel in the apo-state determined by single-particle cryo-electron microscopy at a nominal resolution of 4.3 Å. In this conformation, the ligand-binding domain adopts a conformation reminiscent of the unliganded state with the pore domain captured in a closed conformation. In comparison to the 5-HTR crystal structure, the full-length channel in the apo-conformation adopts a more expanded conformation of all the three domains with a characteristic twist that is implicated in gating.

PubMed: 29410406
DOI: 10.1038/s41467-018-02997-4

Experimental method

ELECTRON MICROSCOPY (4.31 Å)