ReviewJournal of computer-aided molecular design1999
Structural organization of G-protein-coupled receptors.
Review in Journal of computer-aided molecular design, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
16 citing papers in PubMed, 58 citations in OpenAlex.
- Structural Space of the Duffy Antigen/Receptor for Chemokines' Intrinsically Disordered Ectodomain 1 Explored by Temperature Replica-Exchange Molecular Dynamics Simulations.International journal of molecular sciences · 2023Article
- High- and low-affinity sites for sodium in δ-OR-Gi1α (Cys (351)-Ile (351)) fusion protein stably expressed in HEK293 cells; functional significance and correlation with biophysical state of plasma membrane.Naunyn-Schmiedeberg's archives of pharmacology · 2014Article
- Comparative domain modeling of human EGF-like module EMR2 and study of interaction of the fourth domain of EGF with chondroitin 4-sulphate.Journal of biomedical research · 2011Article
- FoldGPCR: structure prediction protocol for the transmembrane domain of G protein-coupled receptors from class A.Proteins · 2010Article
- Human Cytomegalovirus US28: a functionally selective chemokine binding receptor.Infectious disorders drug targets · 2009Review
- The evolution of vertebrate opioid receptors.Frontiers in bioscience (Landmark edition) · 2009Review
- Comparative docking study of anibamine as the first natural product CCR5 antagonist in CCR5 homology models.Journal of chemical information and modeling · 2009Article
- Modelling the structures of G protein-coupled receptors aided by three-dimensional validation.BMC bioinformatics · 2008Article
- The chemokine receptor homologue encoded by US27 of human cytomegalovirus is heavily glycosylated and is present in infected human foreskin fibroblasts and enveloped virus particles.Virus research · 2007Article
- Homology modeling of opioid receptor-ligand complexes using experimental constraints.The AAPS journal · 2005Review
- Membrane model for the G-protein-coupled receptor rhodopsin: hydrophobic interface and dynamical structure.Biophysical journal · 2004Article
- First principles predictions of the structure and function of g-protein-coupled receptors: validation for bovine rhodopsin.Biophysical journal · 2004Article
- Interatomic potentials and solvation parameters from protein engineering data for buried residues.Protein science : a publication of the Protein Society · 2002Article
- Molecular dynamics of 5-HT1A and 5-HT2A serotonin receptors with methylated buspirone analogues.Journal of computer-aided molecular design · 2001Article
- The role of the hydrophilic Asn230 residue of the mu-opioid receptor in the potency of various opioid agonists.British journal of pharmacology · 2001Article
- A sequence and structural study of transmembrane helices.Journal of computer-aided molecular design · 2001Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Atomic-resolution structures of the transmembrane 7-alpha-helical domains of 26 G-protein-coupled receptors (GPCRs) (including opsins, cationic amine, melatonin, purine, chemokine, opioid, and glycoprotein hormone receptors and two related proteins, retinochrome and Duffy erythrocyte antigen) were calculated by distance geometry using interhelical hydrogen bonds formed by various proteins from the family and collectively applied as distance constraints, as described previously [Pogozheva et al., Biophys. J., 70 (1997) 1963]. The main structural features of the calculated GPCR models are described and illustrated by examples. Some of the features reflect physical interactions that are responsible for the structural stability of the transmembrane alpha-bundle: the formation of extensive networks of interhelical H-bonds and sulfur-aromatic clusters that are spatially organized as 'polarity gradients'; the close packing of side-chains throughout the transmembrane domain; and the formation of interhelical disulfide bonds in some receptors and a plausible Zn2+ binding center in retinochrome. Other features of the models are related to biological function and evolution of GPCRs: the formation of a common 'minicore' of 43 evolutionarily conserved residues; a multitude of correlated replacements throughout the transmembrane domain; an Na(+)-binding site in some receptors, and excellent complementarity of receptor binding pockets to many structurally dissimilar, conformationally constrained ligands, such as retinal, cyclic opioid peptides, and cationic amine ligands. The calculated models are in good agreement with numerous experimental data.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.