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Article

Communication between the ERRalpha homodimer interface and the PGC-1alpha binding surface via the helix 8-9 loop.

The Journal of biological chemistry - 18 Jul 2008

Greschik Holger, Althage Magnus, Flaig Ralf, Sato Yoshiteru, Chavant Virginie, Peluso-Iltis Carole, Choulier Laurence, Cronet Philippe, Rochel Natacha, Schüle Roland, Strömstedt Per-Erik, Moras Dino

Abstract excerpt

Although structural studies on the ligand-binding domain (LBD) have established the general mode of nuclear receptor (NR)/coactivator interaction, determinants of binding specificity are only partially understood. The LBD of estrogen receptor-alpha (ERalpha), for example, interacts only with a region of peroxisome proliferator-activated receptor coactivator (PGC)-1alpha, which contains the canonical LXXLL motif...

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Share to Crystallography, X-Ray
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heat-Shock Proteins

Share to Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha

Share to Protein Structure, Quaternary

Share to Protein Structure, Secondary

Share to Receptors, Estrogen

Share to Sequence Alignment

Source

Identifiers

PMID: 18441008
DOI: 10.1074/jbc.M801920200

Genes

PGC

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Communication between the ERRalpha homodimer interface and the PGC-1alpha binding surface via the helix 8-9 loop.PMID 18441008Read ↗

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