Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Evolutionary identification of a subtype specific functional site in the ligand binding domain of steroid receptors.

Proteins - 1 Sept 2006

Raviscioni Michele, He Qiang, Salicru Eleni M, Smith Carolyn L, Lichtarge Olivier

Abstract excerpt

Nuclear receptors are ubiquitous eukaryotic ligand-activated transcription factors that modulate gene expression through varied interactions. However, the highly conserved functional sites known today seem insufficient to explain receptor specific recruitment of different coactivator and corepressor proteins and regulation of transcription. To search for new receptor-subtype specific functional sites, we applied...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Allosteric Site
Share to Amino Acid Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Binding Sites

Share to Evolution, Molecular

Share to HeLa Cells

Share to Ligands

Share to Models, Molecular

Share to Receptors, Estrogen

Source

Identifiers

PMID: 16835908
DOI: 10.1002/prot.21074

Genes

SRC

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evolutionary identification of a subtype specific functional site in the ligand binding domain of steroid receptors.PMID 16835908Read ↗

Structural evolution of the estrogen receptor regulatory domainSemantic proximity Read ↗

A comprehensive structural and functional analysis of the ligand binding domain of the nuclear receptor superfamily reveals highly conserved signaling motifs and two distinct canonical forms through evolutionSemantic proximity Read ↗

Rewiring Ancient Residue Interaction Networks Drove the Evolution of Specificity in Steroid Receptors.Semantic proximity Read ↗

A conserved surface on the ligand binding domain of nuclear receptors for allosteric control.Semantic proximity Read ↗

Biophysical mechanisms for large-effect mutations in the evolution of steroid hormone receptors.Semantic proximity Read ↗

A Structural Signature Motif Enlightens the Origin and Diversification of Nuclear ReceptorsSemantic proximity Read ↗

Vestigialization of an allosteric switch: genetic and structural mechanisms for the evolution of constitutive activity in a steroid hormone receptor.Semantic proximity Read ↗

Structural determinants of allosteric ligand activation in RXR heterodimers.Semantic proximity Read ↗

Evolution of the repertoire of nuclear receptor binding sites in genomes.Semantic proximity Read ↗

Natural disordered sequences in the amino terminal domain of nuclear receptors: lessons from the androgen and glucocorticoid receptors.Semantic proximity Read ↗

A family-based approach reveals the function of residues in the nuclear receptor ligand-binding domain.Semantic proximity Read ↗

Asymmetric Cross-Reactivity of Nuclear Receptors Reveals an Evolutionary Buffer Between Estrogen and Androgen SignalingSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.