Evidence map›Paper›PMID 20512150›Full record

ArticleNature structural & molecular biology2010

Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy.

Antoine Gautier, Helen R Mott, Mark J Bostock, John P Kirkpatrick, Daniel Nietlispach

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
–field-weighted citation impact
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

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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

83 citing papers in PubMed.

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  7. GPCR structural characterization by NMR spectroscopy in solution.Acta biochimica et biophysica Sinica · 2022
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23 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Antoine GautierDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Helen R Mott
Mark J Bostock
John P Kirkpatrick
Daniel Nietlispach

Funding

Biotechnology and Biological Sciences Research Council BB/E013228/1Biotechnology and Biological Sciences Research Council BB/G011915/1Cancer Research UKWellcome Trust
6 · The paper itself

Abstract

Seven-helix membrane proteins represent a challenge for structural biology. Here we report the first NMR structure determination of a detergent-solubilized seven-helix transmembrane (7TM) protein, the phototaxis receptor sensory rhodopsin II (pSRII) from Natronomonas pharaonis, as a proof of principle. The overall quality of the structure ensemble is good (backbone r.m.s. deviation of 0.48 A) and agrees well with previously determined X-ray structures. Furthermore, measurements in more native-like small phospholipid bicelles indicate that the protein structure is the same as in detergent micelles, suggesting that environment-specific effects are minimal when using mild detergents. We use our case study as a platform to discuss the feasibility of similar solution NMR studies for other 7TM proteins, including members of the family of G protein-coupled receptors.

Indexed as

DetergentsHalobacteriaceaeHalorhodopsinsHydrophobic and Hydrophilic InteractionsMicellesModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein StabilityProtein Structure, SecondaryReceptors, G-Protein-CoupledSensory RhodopsinsSolubilityThermodynamicsDetergentsHalorhodopsinsMicellesReceptors, G-Protein-Coupledsensory rhodopsin II protein, archaealSensory Rhodopsins

Identifiers

PMID20512150
PMCPMC2923064

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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.