Evidence map›Paper›PMID 24564869›Full record

ArticleBMC genomics2013

Residue correlation networks in nuclear receptors reflect functional specialization and the formation of the nematode-specific P-box.

Marcelo Querino Lima Afonso, Leonardo Henrique França de Lima, Lucas Bleicher

Abstract read
In one paragraph

Article in BMC genomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

3 authors.

Marcelo Querino Lima Afonso
Leonardo Henrique França de Lima
Lucas Bleicher

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundNuclear receptors (NRs) are transcription factors which bind small hormones, whose evolutionary history and the presence of different functional surfaces makes them an interesting target for a correlation based analysis.

resultsCorrelation analysis of ligand binding domains shows that correlated residue subsets arise from the differences between functional sites in different nuclear receptor subfamilies. For the DNA binding domain, particularly, the analysis shows that the main source of correlation comes from residues that regulate hormone response element specificity, and one of the conserved residue sub-sets arises due to the presence of an unusual sequence for the DNA binding motif known as P-box in nematodes, suggesting the existence of different DBD-DNA specificities in nuclear receptors.

conclusionsWe conclude that DNA specificity and functional surface specialization has independently driven nuclear receptor evolution, and suggest possible binding modes for the class of divergent nuclear receptors in nematodes.

Indexed as

Amino Acid MotifsAmino AcidsAmino Acid SubstitutionAnimalsDNADNA-Binding ProteinsHelminth ProteinsLigandsModels, MolecularNematodaProtein BindingProtein Interaction MapsProtein Structure, TertiaryReceptors, Cytoplasmic and NuclearSpecies SpecificityAmino AcidsDNADNA-Binding ProteinsHelminth ProteinsLigandsReceptors, Cytoplasmic and Nuclear

Identifiers

PMID24564869
PMCPMC3908500

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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.