Evidence map›Paper›PMID 27030110›Full record

ArticleThe Journal of biological chemistry2016

Insights into the C-terminal Peptide Binding Specificity of the PDZ Domain of Neuronal Nitric-oxide Synthase: CHARACTERIZATION OF THE INTERACTION WITH THE TIGHT JUNCTION PROTEIN CLAUDIN-3.

Javier Merino-Gracia, Carlos Costas-Insua, María Ángeles Canales, Ignacio Rodríguez-Crespo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Human Serine Racemase Weakly Binds the Third PDZ Domain of PSD-95.International journal of molecular sciences · 2022
    Article
  5. Identification of BiP as a CBThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
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  7. Article
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  9. Article
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  11. Review
  12. 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 at 2 institutions in 1 country.

Javier Merino-GraciaFrom the Departamentos de Bioquímica y Biología Molecular and.
Carlos Costas-InsuaFrom the Departamentos de Bioquímica y Biología Molecular and.
María Ángeles CanalesQuímica Orgánica, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid 28040, Spain.
Ignacio Rodríguez-CrespoFrom the Departamentos de Bioquímica y Biología Molecular and nacho@bbm1.ucm.es.
Centro de Biología Molecular Severo Ochoa · ESUniversidad Complutense de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neuronal nitric-oxide synthase, unlike its endothelial and inducible counterparts, displays a PDZ (PSD-95/Dlg/ZO-1) domain located at its N terminus involved in subcellular targeting. The C termini of various cellular proteins insert within the binding groove of this PDZ domain and determine the subcellular distribution of neuronal NOS (nNOS). The molecular mechanisms underlying these interactions are poorly understood because the PDZ domain of nNOS can apparently exhibit class I, class II, and class III binding specificity. In addition, it has been recently suggested that the PDZ domain of nNOS binds with very low affinity to the C termini of target proteins, and a necessary simultaneous lateral interaction must take place for binding to occur. We describe herein that the PDZ domain of nNOS can behave as a bona fide class III PDZ domain and bind to C-terminal sequences with acidic residues at the P-2 position with low micromolar binding constants. Binding to C-terminal sequences with a hydrophobic residue at the P-2 position plus an acidic residue at the P-3 position (class II) can also occur, although interactions involving residues extending up to the P-7 position mediate this type of binding. This promiscuous behavior also extends to its association to class I sequences, which must display a Glu residue at P-3 and a Thr residue at P-2 By means of site-directed mutagenesis and NMR spectroscopy, we have been able to identify the residues involved in each specific type of binding and rationalize the mechanisms used to recognize binding partners. Finally, we have analyzed the high affinity association of the PDZ domain of nNOS to claudin-3 and claudin-14, two tight junction tetraspan membrane proteins that are essential components of the paracellular barrier.

Indexed as

PDZ DomainsAmino Acid SequenceAnimalsBinding SitesCells, CulturedClaudin-3Fluorescence PolarizationFluorescent Antibody TechniqueImmunoprecipitationMagnetic Resonance SpectroscopyMolecular Sequence DataMutagenesis, Site-DirectedNeuronsNitric Oxide Synthase Type IPeptide FragmentsProtein BindingClaudin-3Nitric Oxide Synthase Type INos1 protein, ratPeptide Fragmentsnitric oxidenitric oxide synthasenuclear magnetic resonance (NMR)PDZ domainprotein-protein interactiontight junction

Identifiers

PMID27030110
PMCPMC4882429
OpenAlexW2326178713

What OpenQuestion holds

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Registered trials

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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.