Evidence map›Paper›PMID 21645852›Full record

ArticleStructure (London, England : 1993)2011

Domain orientation in the N-Terminal PDZ tandem from PSD-95 is maintained in the full-length protein.

James J McCann, Liqiang Zheng, Salvatore Chiantia, Mark E Bowen

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Molecular and Spectroscopic Characterization of Green and Red Cyanine Fluorophores from the Alexa Fluor and AF Series*.Chemphyschem : a European journal of chemical physics and physical chemistry · 2021
    Article
  6. Article
  7. Supertertiary protein structure affects an allosteric network.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Emerging Themes in PDZ Domain Signaling: Structure, Function, and Inhibition.International review of cell and molecular biology · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Supertertiary structure of the synaptic MAGuK scaffold proteins is conserved.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  18. Article
  19. 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.

James J McCannDepartment of Pharmacological Sciences, Stony Brook University, Stony Brook, NY 11794, USA.
Liqiang Zheng
Salvatore Chiantia
Mark E Bowen

Funding

SINGLE MOLECULE ANALYSIS OF PSD-95 STRUCTURE AND LIGAND BINDINGR01MH081923 · NIMH · STATE UNIVERSITY NEW YORK STONY BROOK · PI BOWEN, MARK E · 2008 to 2022
$5.6M
Training Program in Pharmacological SciencesT32GM007518 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI GARCIA-DIAZ, MIGUEL · 1985 to 2021
$5.4M
NIGMS NIH HHS T32 GM007518NIMH NIH HHS MH081923NIMH NIH HHS R01 MH081923
6 · The paper itself

Abstract

Tandem PDZ domains have been suggested to form structurally independent supramodules. However, dissimilarity between crystallography and NMR models emphasize their malleable conformation. Studies in full-length scaffold proteins are needed to examine the effect of tertiary interactions within their native context. Using single-molecule fluorescence to characterize the N-terminal PDZ tandem in PSD-95, we provide the first direct evidence that PDZ tandems can be structurally independent within a full-length scaffold protein. Molecular refinement using our data converged on a single structure with an antiparallel alignment of the ligand-binding sites. Devoid of interaction partners, single-molecule conditions captured PSD-95 in its unbound, ground state. Interactions between PDZ domains could not be detected while fluctuation correlation spectroscopy showed that other conformations are dynamically sampled. We conclude that ultra-weak interactions stabilize the conformation providing a "low-relief" energy landscape that allows the domain orientation to be flipped by environmental interactions.

Indexed as

Amino Acid SequenceAnimalsCysteineDisks Large Homolog 4 ProteinFluorescence Resonance Energy TransferIntracellular Signaling Peptides and ProteinsMembrane ProteinsMolecular Dynamics SimulationPeptide FragmentsProtein Structure, TertiaryRatsRecombinant ProteinsCysteineDisks Large Homolog 4 ProteinDlg4 protein, ratIntracellular Signaling Peptides and ProteinsMembrane ProteinsPeptide FragmentsRecombinant Proteins

Identifiers

PMID21645852
PMCPMC3116789

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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.