Evidence map›Paper›PMID 18462673›Full record

ArticleStructure (London, England : 1993)2008

Crystal structure of NFAT bound to the HIV-1 LTR tandem kappaB enhancer element.

Darren L Bates, Kristen K B Barthel, Yongqing Wu, Reza Kalhor, James C Stroud, Michael J Giffin, Lin Chen

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

24 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  18. NF-κB/Rel: agonist and antagonist roles in HIV-1 latency.Current opinion in HIV and AIDS · 2011
    Review
  19. Article
  20. Review
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

7 authors at 2 institutions in 1 country.

Darren L BatesDepartment of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309-0215, USA.
Kristen K B Barthel
Yongqing Wu
Reza Kalhor
James C Stroud
Michael J Giffin
Lin Chen
University of Colorado Boulder · USUniversity of Southern California · US

Funding

TRAINING IN SIGNAL TRANSDUCTION &CELL CYCLE REGULATIONT32GM008759 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI AHN, NATALIE G. · 2000 to 2020
$5.9M
Predoctoral Training Program in Signaling and Cellular Regulation INCLUDE Down Syndrome SupplementT32GM142607 · NIGMS · UNIVERSITY OF COLORADO · PI Sabrina Leigh Spencer, Tin Tin Su · 2021 to 2026
$3.6M
Structural and Functional Versatility of NFATR01GM064642 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, LIN · 2005 to 2014
$2.5M
NIGMS NIH HHS R01 GM064642NIGMS NIH HHS T32 GM008759NIGMS NIH HHS T32 GM142607
6 · The paper itself

Abstract

The host factor, nuclear factor of activated T-cells (NFAT), regulates the transcription and replication of HIV-1. Here, we have determined the crystal structure of the DNA binding domain of NFAT bound to the HIV-1 long terminal repeat (LTR) tandem kappaB enhancer element at 3.05 A resolution. NFAT binds as a dimer to the upstream kappaB site (Core II), but as a monomer to the 3' end of the downstream kappaB site (Core I). The DNA shows a significant bend near the 5' end of Core I, where a lysine residue from NFAT bound to the 3' end of Core II inserts into the minor groove and seems to cause DNA bases to flip out. Consistent with this structural feature, the 5' end of Core I become hypersensitive to dimethylsulfate in the in vivo footprinting upon transcriptional activation of the HIV-1 LTR. Our studies provide a basis for further investigating the functional mechanisms of NFAT in HIV-1 transcription and replication.

Indexed as

Enhancer Elements, GeneticBinding SitesComputer SimulationCrystallography, X-RayDNAHIV-1HIV Long Terminal RepeatHumansModels, MolecularNFATC Transcription FactorsNF-kappa BNucleic Acid ConformationProtein Structure, TertiaryRecombinant ProteinsDNANFATC1 protein, humanNFATC Transcription FactorsNF-kappa BRecombinant Proteins

Identifiers

PMID18462673
PMCPMC2697820
OpenAlexW2140124506

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.