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Structure paper

TitleCryo-EM structure of 5-HT receptor in its resting conformation.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 514, Year 2018
Publish dateFeb 6, 2018
AuthorsSandip Basak / Yvonne Gicheru / Amrita Samanta / Sudheer Kumar Molugu / Wei Huang / Maria la de Fuente / Taylor Hughes / Derek J Taylor / Marvin T Nieman / Vera Moiseenkova-Bell / Sudha Chakrapani /
PubMed AbstractSerotonin 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. ...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.
External linksNat Commun / PubMed:29410406 / PubMed Central
MethodsEM (single particle)
Resolution4.31 Å
Structure data

7088

6be1

EMDB-7088, PDB-6be1:
Cryo-EM structure of serotonin receptor
Method: EM (single particle) / Resolution: 4.31 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-NA:
Unknown entry

ChemComp-PX4:
1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DMPC, phospholipid*YM

ChemComp-CL:
Unknown entry

ChemComp-BMA:
beta-D-mannopyranose

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / Ion Channel

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