What the research shows
Researchers used nuclear magnetic resonance spectroscopy to determine the three-dimensional shape of the DNA-binding region of human FOXO4 in solution. They found a folded region resembling those of several other forkhead transcription factors. The measurement covered one domain, which is a portion of the protein with a particular function. Solution structure of the human FOXO4 DNA-binding domain.
The curated human sequence record identifies FOXO4 and its protein features, providing a reference for identifying which portion a structural study used. UniProt human FOXO4 sequence record.
Documented formats
The structural study used an isolated protein domain. The reviewed human FOXO4 sequence is recorded under UniProt accession P98177. A short inhibitor designed around a FOXO4 interaction is another material.
Testing and purity
Match the organism, sequence accession, and first and last residues of the study construct. Check for a purification tag or other extra sequence before comparing the expected mass.
How to read a batch reportQuestions about FOXO4
Why can two papers report different sizes for FOXO4?
One laboratory may work with full-length protein and another with only its DNA-binding region. The construct boundaries identify the material measured.
Does FOXO4 mean FOXO4-DRI?
FOXO4 identifies the natural protein. FOXO4-DRI identifies an engineered peptide developed to interfere with one of that protein’s interactions.