ArticleBMC biochemistry2002
Identification of critical residues in loop E in the 5-HT3ASR binding site.
Article in BMC biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Article
- Structure, Function and Physiology of 5-Hydroxytryptamine Receptors Subtype 3.Sub-cellular biochemistry · 2021Review
- The binding characteristics and orientation of a novel radioligand with distinct properties at 5-HT3A and 5-HT3AB receptors.Neuropharmacology · 2014Article
- 5-HT(3) receptors.The Journal of biological chemistry · 2012Review
- Design, synthesis, and structure-activity relationships of highly potent 5-HT₃ receptor ligands.Journal of medicinal chemistry · 2012Article
- Cysteine modification reveals which subunits form the ligand binding site in human heteromeric 5-HT3AB receptors.The Journal of physiology · 2011Article
- Therapeutics of 5-HT3 receptor antagonists: current uses and future directions.Pharmacology & therapeutics · 2011Review
- Mapping spatial relationships between residues in the ligand-binding domain of the 5-HT3 receptor using a molecular ruler.Biophysical journal · 2010Article
- Gating mechanisms in Cys-loop receptors.European biophysics journal : EBJ · 2009Review
- The 5-HT3 receptor--the relationship between structure and function.Neuropharmacology · 2009Review
- 5-HT3 receptors.Current pharmaceutical design · 2006Review
- Tyrosine residues that control binding and gating in the 5-hydroxytryptamine3 receptor revealed by unnatural amino acid mutagenesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004Article
- Subunit rotation models activation of serotonin 5-HT3AB receptors by agonists.Journal of computer-aided molecular design · 2004Article
- Prediction of 5-HT3 receptor agonist-binding residues using homology modeling.Biophysical journal · 2003Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe serotonin type 3 receptor (5-HT3R) is a member of a superfamily of ligand gated ion channels. All members of this family share a large degree of sequence homology and presumably significant structural similarity. A large number of studies have explored the structure-function relationships of members of this family, particularly the nicotinic and GABA receptors. This information can be utilized to gain additional insights into specific structural and functional features of other receptors in this family.
resultsThirteen amino acids in the mouse 5-HT3ASR that correspond to the putative E binding loop of the nicotinic alpha7 receptor were chosen for mutagenesis. Due to the presence of a highly conserved glycine in this region, it has been suggested that this binding loop is comprised of a hairpin turn and may form a portion of the ligand-binding site in this ion channel family. Mutation of the conserved glycine (G147) to alanine eliminated binding of the 5-HT3R antagonist [3H]granisetron. Three tyrosine residues (Y140, Y142 and Y152) also significantly altered the binding of 5-HT3R ligands. Mutations in neighboring residues had little or no effect on binding of these ligands to the 5-HT3ASR.
conclusionOur data supports a role for the putative E-loop region of the 5-HT3R in the binding of 5-HT, mCPBG, d-tc and lerisetron. 5-HT and mCPBG interact with Y142, d-tc with Y140 and lerisetron with both Y142 and Y152. Our data also provides support for the hypothesis that this region of the receptor is present in a loop structure.
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