ArticleBiophysical journal1998
A proposed structure for transmembrane segment 7 of G protein-coupled receptors incorporating an asn-Pro/Asp-Pro motif.
Article in Biophysical journal, 1998. 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
- Search for Structural Basis of Interactions of Biogenic Amines with Human TAAR1 and TAAR6 Receptors.International journal of molecular sciences · 2021Article
- Advances in therapeutic peptides targeting G protein-coupled receptors.Nature reviews. Drug discovery · 2020Review
- Orphan G-protein coupled receptor 22 (Gpr22) regulates cilia length and structure in the zebrafish Kupffer's vesicle.PloS one · 2014Article
- Palmitoylation and membrane cholesterol stabilize μ-opioid receptor homodimerization and G protein coupling.BMC cell biology · 2012Article
- Identification of specific transmembrane residues and ligand-induced interface changes involved in homo-dimer formation of a yeast G protein-coupled receptor.Biochemistry · 2009Article
- Solid-state NMR and molecular dynamics characterization of cannabinoid receptor-1 (CB1) helix 7 conformational plasticity in model membranes.Biochimica et biophysica acta · 2009Article
- Generation of a homology model of the human histamine H(3) receptor for ligand docking and pharmacophore-based screening.Journal of computer-aided molecular design · 2007Article
- Identification of the hydrophobic ligand binding pocket of the S1P1 receptor.The Journal of biological chemistry · 2007Article
- A strategy using NMR peptide structures of thromboxane A2 receptor as templates to construct ligand-recognition pocket of prostacyclin receptor.BMC biochemistry · 2005Article
- New insights into the human 5-HT4 receptor binding site: exploration of a hydrophobic pocket.British journal of pharmacology · 2004Article
- Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin.Biochemistry · 2003Review
- A single amino acid substitution (N297A) in the conserved NPXXY sequence of the human N-formyl peptide receptor results in inhibition of desensitization and endocytosis, and a dose-dependent shift in p42/44 mitogen-activated protein kinase activation and chemotaxis.The Biochemical journal · 2000Article
- Modeling and docking the endothelin G-protein-coupled receptor.Biophysical journal · 2000Article
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4 authors.
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Abstract
Transmembrane segment (TMS) 7 has been shown to play an important role in the signal transduction function of G-protein-coupled receptors (GPCRs). Although transmembrane segments are most likely to adopt a helical structure, results from a variety of experimental studies involving TMS 7 are inconsistent with it being an ideal alpha-helix. Using results from a search of the structure database and extensive simulated annealing Monte Carlo runs with the new Conformational Memories method, we have identified the conserved (N/D)PxxY region of TMS 7 as the major determinant for deviation of TMS 7 from ideal helicity. The perturbation consists of an Asx turn and a flexible "hinge" region. The Conformational Memories procedure yielded a model structure of TMS 7 which, unlike an ideal alpha-helix, is capable of accommodating all of the experimentally derived geometrical criteria for the interactions of TMS 7 in the transmembrane bundle of GPCRs. In the context of the entire structure of a transmembrane bundle model for the 5HT2a receptor, the specific perturbation of TMS 7 by the NP sequence suggests a structural hypothesis for the pattern of amino acid conservation observed in TMS 1, 2, and 7 of GPCRs. The structure resulting from the incorporation of the (N/D)P motif satisfies fully the H-bonding capabilities of the 100% conserved polar residues in these TMSs, in agreement with results from mutagenesis experiments. The flexibility introduced by the specific structural perturbation produced by the (NP/DP) motif in TMS 7 is proposed to have a significant role in receptor activation.
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