Evidence map›Paper›PMID 20441771›Full record

ArticleBiochimica et biophysica acta2010

NMR structure of the transmembrane domain of the n-acetylcholine receptor beta2 subunit.

Vasyl Bondarenko, Tommy Tillman, Yan Xu, Pei Tang

Abstract readComparative Study
In one paragraph

Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

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

16 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Highly Coarse-Grained Representations of Transmembrane Proteins.Journal of chemical theory and computation · 2017
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
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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.

Vasyl BondarenkoDepartment of Anesthesiology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Tommy Tillman
Yan Xu
Pei Tang

Funding

NMR STUDIES OF MECHANISMS OF GENERAL ANESTHESIAR37GM049202 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI XU, YAN · 2004 to 2013
$4.9M
ANESTHETIC SITES IN TRANSMEMBRANE PEPTIDES BY NMRR01GM056257 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI TANG, PEI · 1998 to 2017
$4.8M
ANESTHETIC EFFECTS ON ION CHANNEL STRUCTURES & DYNAMICSR01GM066358 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI TANG, PEI · 2002 to 2014
$3.6M
NIGMS NIH HHS R01 GM056257NIGMS NIH HHS R01 GM066358NIGMS NIH HHS R01GM56257NIGMS NIH HHS R01GM66358NIGMS NIH HHS R37 GM049202NIGMS NIH HHS R37GM049202
6 · The paper itself

Abstract

Nicotinic acetylcholine receptors (nAChRs) are involved in fast synaptic transmission in the central and peripheral nervous system. Among the many different types of subunits in nAChRs, the beta2 subunit often combines with the alpha4 subunit to form alpha4beta2 pentameric channels, the most abundant subtype of nAChRs in the brain. Besides computational predictions, there is limited experimental data available on the structure of the beta2 subunit. Using high-resolution NMR spectroscopy, we solved the structure of the entire transmembrane domain (TM1234) of the beta2 subunit. We found that TM1234 formed a four-helix bundle in the absence of the extracellular and intracellular domains. The structure exhibited many similarities to those previously determined for the Torpedo nAChR and the bacterial ion channel GLIC. We also assessed the influence of the fourth transmembrane helix (TM4) on the rest of the domain. Although secondary structures and tertiary arrangements were similar, the addition of TM4 caused dramatic changes in TM3 dynamics and subtle changes in TM1 and TM2. Taken together, this study suggests that the structures of the transmembrane domains of these proteins are largely shaped by determinants inherent in their sequence, but their dynamics may be sensitive to modulation by tertiary and quaternary contacts.

Indexed as

Amino Acid SequenceAnimalsHumansModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein Structure, SecondaryProtein Structure, TertiaryReceptors, NicotinicRecombinant Fusion ProteinsSpecies SpecificityStructural Homology, ProteinTorpedoPeptide FragmentsReceptors, NicotinicRecombinant Fusion Proteins

Identifiers

PMID20441771
PMCPMC2885491

What OpenQuestion holds

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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.