Evidence map›Paper›PMID 16131665›Full record

ArticleProtein science : a publication of the Protein Society2005

Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha.

Jason R Schnell, Guo-Ping Zhou, Markus Zweckstetter, Alan C Rigby, James J Chou

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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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3 · Its place in the literature

Who cites it

22 citing papers in PubMed.

  1. Article
  2. Redox Regulation of KAntioxidants & redox signaling · 2024
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  19. Assignment-free solution NMR method reveals CesT as an unswapped homodimer.Protein science : a publication of the Protein Society · 2008
    Article
  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

5 authors.

Jason R SchnellDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Guo-Ping Zhou
Markus Zweckstetter
Alan C Rigby
James J Chou

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Coiled-coil motifs play essential roles in protein assembly and molecular recognition, and are therefore the targets of many ongoing structural and functional studies. However, owing to the dynamic nature of many of the smaller coiled-coil domains, crystallization for X-ray studies is very challenging. Determination of elongated structures using standard NMR approaches is inefficient and usually yields low-resolution structures due to accumulation of small errors over long distances. Here we describe a solution NMR approach based on residual dipolar couplings (RDCs) for rapid and accurate structure determination of coiled-coil dimers. Using this approach, we were able to determine the high-resolution structure of the coiled-coil domain of cGMP-dependent protein kinase Ialpha, a protein of previously unknown structure that is critical for physiological relaxation of vascular smooth muscle. This approach can be extended to solve coiled-coil structures with higher order assemblies.

Indexed as

Models, MolecularAmino Acid SequenceCyclic GMP-Dependent Protein KinasesCyclic GMP-Dependent Protein Kinase Type IDimerizationHumansMagnetic Resonance SpectroscopyMolecular Sequence DataProtein ConformationProtein Structure, TertiaryCyclic GMP-Dependent Protein KinasesCyclic GMP-Dependent Protein Kinase Type IPRKG1 protein, human

Identifiers

PMID16131665
PMCPMC2253468

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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.