Evidence map›Paper›PMID 15966721›Full record

ArticleBiochemistry2005

Comparison of class A and D G protein-coupled receptors: common features in structure and activation.

Markus Eilers, Viktor Hornak, Steven O Smith, James B Konopka

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.2field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. A Paradigm for Peptide Hormone-GPCR Analyses.Molecules (Basel, Switzerland) · 2020
    Review
  5. Article
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  13. Review
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  18. Article
  19. Fungal mating pheromones: choreographing the dating game.Fungal genetics and biology : FG & B · 2011
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Markus EilersDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794-5222, USA.
Viktor Hornak
Steven O Smith
James B Konopka
Stony Brook University · US

Funding

Structure and Activation Mechanism of the Visual Pigment RhodopsinR01GM041412 · NIGMS · YALE UNIVERSITY · PI SMITH, STEVEN OWEN · 1989 to 2014
$4.4M
ACTIVATION OF G PROTEIN COUPLED RECEPTORSR01GM055107 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI KONOPKA, JAMES B. · 1997 to 2004
$1.2M
NIGMS NIH HHS GM-41412NIGMS NIH HHS GM55107NIGMS NIH HHS R01 GM041412NIGMS NIH HHS R01 GM055107
6 · The paper itself

Abstract

All G protein-coupled receptors (GPCRs) share a common seven TM helix architecture and the ability to activate heterotrimeric G proteins. Nevertheless, these receptors have widely divergent sequences with no significant homology. We present a detailed structure-function comparison of the very divergent Class A and D receptors to address whether there is a common activation mechanism across the GPCR superfamily. The Class A and D receptors are represented by the vertebrate visual pigment rhodopsin and the yeast alpha-factor pheromone receptor Ste2, respectively. Conserved amino acids within each specific receptor class and amino acids where mutation alters receptor function were located in the structures of rhodopsin and Ste2 to assess whether there are functionally equivalent positions or regions within these receptors. We find several general similarities that are quite striking. First, strongly polar amino acids mediate helix interactions. Their mutation generally leads to loss of function or constitutive activity. Second, small and weakly polar amino acids facilitate tight helix packing. Third, proline is essential at similar positions in transmembrane helices 6 and 7 of both receptors. Mapping the specific location of the conserved amino acids and sites of constitutively active mutations identified conserved microdomains on transmembrane helices H3, H6, and H7, suggesting that there are underlying similarities in the mechanism of the widely divergent Class A and Class D receptors.

Indexed as

Amino Acid SequenceConserved SequenceCrystallography, X-RayFungal ProteinsHydrogen BondingHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular Sequence DataProtein Structure, SecondaryReceptors, G-Protein-CoupledRhodopsinSequence AlignmentStructure-Activity RelationshipFungal ProteinsReceptors, G-Protein-CoupledRhodopsin

Identifiers

PMID15966721
PMCPMC1382269
OpenAlexW2037969148

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.